HRAS | ENSG00000174775 | NCBI 3265

Details for: HRAS

Gene ID: 3265

Symbol: HRAS

Ensembl ID: ENSG00000174775

Description: HRas proto-oncogene, GTPase

Associated with

Activation of nmda receptors and postsynaptic events
(R-HSA-442755)
Adaptive immune system
(R-HSA-1280218)
Axon guidance
(R-HSA-422475)
C-type lectin receptors (clrs)
(R-HSA-5621481)
Cd209 (dc-sign) signaling
(R-HSA-5621575)
Cell surface interactions at the vascular wall
(R-HSA-202733)
Constitutive signaling by overexpressed erbb2
(R-HSA-9634285)
Cytokine signaling in immune system
(R-HSA-1280215)
Dap12 interactions
(R-HSA-2172127)
Dap12 signaling
(R-HSA-2424491)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Downstream signaling events of b cell receptor (bcr)
(R-HSA-1168372)
Downstream signal transduction
(R-HSA-186763)
Eph-ephrin signaling
(R-HSA-2682334)
Erythropoietin activates ras
(R-HSA-9027284)
Esr-mediated signaling
(R-HSA-8939211)
Extra-nuclear estrogen signaling
(R-HSA-9009391)
Fc epsilon receptor (fceri) signaling
(R-HSA-2454202)
Fceri mediated mapk activation
(R-HSA-2871796)
Flt3 signaling
(R-HSA-9607240)
Flt3 signaling in disease
(R-HSA-9682385)
G alpha (q) signalling events
(R-HSA-416476)
Gpcr downstream signalling
(R-HSA-388396)
Grb2 events in egfr signaling
(R-HSA-179812)
Grb2 events in erbb2 signaling
(R-HSA-1963640)
Hemostasis
(R-HSA-109582)
Igf1r signaling cascade
(R-HSA-2428924)
Immune system
(R-HSA-168256)
Innate immune system
(R-HSA-168249)
Insulin receptor signalling cascade
(R-HSA-74751)
Mapk1/mapk3 signaling
(R-HSA-5684996)
Mapk family signaling cascades
(R-HSA-5683057)
Met activates ras signaling
(R-HSA-8851805)
Ncam signaling for neurite out-growth
(R-HSA-375165)
Nervous system development
(R-HSA-9675108)
Neuronal system
(R-HSA-112316)
Neurotransmitter receptors and postsynaptic signal transmission
(R-HSA-112314)
Oncogenic mapk signaling
(R-HSA-6802957)
Paradoxical activation of raf signaling by kinase inactive braf
(R-HSA-6802955)
Ptk6 regulates rho gtpases, ras gtpase and map kinases
(R-HSA-8849471)
Raf/map kinase cascade
(R-HSA-5673001)
Ras signaling downstream of nf1 loss-of-function variants
(R-HSA-6802953)
Shc1 events in egfr signaling
(R-HSA-180336)
Shc1 events in erbb2 signaling
(R-HSA-1250196)
Shc1 events in erbb4 signaling
(R-HSA-1250347)
Signaling by braf and raf1 fusions
(R-HSA-6802952)
Signaling by egfr
(R-HSA-177929)
Signaling by egfr in cancer
(R-HSA-1643713)
Signaling by egfrviii in cancer
(R-HSA-5637812)
Signaling by erbb2
(R-HSA-1227986)
Signaling by erbb2 ecd mutants
(R-HSA-9665348)
Signaling by erbb2 in cancer
(R-HSA-1227990)
Signaling by erbb2 kd mutants
(R-HSA-9664565)
Signaling by erbb2 tmd/jmd mutants
(R-HSA-9665686)
Signaling by erbb4
(R-HSA-1236394)
Signaling by erythropoietin
(R-HSA-9006335)
Signaling by fgfr
(R-HSA-190236)
Signaling by fgfr1
(R-HSA-5654736)
Signaling by fgfr1 in disease
(R-HSA-5655302)
Signaling by fgfr2
(R-HSA-5654738)
Signaling by fgfr2 in disease
(R-HSA-5655253)
Signaling by fgfr3
(R-HSA-5654741)
Signaling by fgfr3 in disease
(R-HSA-5655332)
Signaling by fgfr4
(R-HSA-5654743)
Signaling by fgfr4 in disease
(R-HSA-5655291)
Signaling by fgfr in disease
(R-HSA-1226099)
Signaling by flt3 fusion proteins
(R-HSA-9703465)
Signaling by flt3 itd and tkd mutants
(R-HSA-9703648)
Signaling by gpcr
(R-HSA-372790)
Signaling by high-kinase activity braf mutants
(R-HSA-6802948)
Signaling by insulin receptor
(R-HSA-74752)
Signaling by kit in disease
(R-HSA-9669938)
Signaling by ligand-responsive egfr variants in cancer
(R-HSA-5637815)
Signaling by met
(R-HSA-6806834)
Signaling by moderate kinase activity braf mutants
(R-HSA-6802946)
Signaling by non-receptor tyrosine kinases
(R-HSA-9006927)
Signaling by ntrk1 (trka)
(R-HSA-187037)
Signaling by ntrk2 (trkb)
(R-HSA-9006115)
Signaling by ntrk3 (trkc)
(R-HSA-9034015)
Signaling by ntrks
(R-HSA-166520)
Signaling by nuclear receptors
(R-HSA-9006931)
Signaling by pdgf
(R-HSA-186797)
Signaling by pdgfra extracellular domain mutants
(R-HSA-9673770)
Signaling by pdgfra transmembrane, juxtamembrane and kinase domain mutants
(R-HSA-9673767)
Signaling by pdgfr in disease
(R-HSA-9671555)
Signaling by phosphorylated juxtamembrane, extracellular and kinase domain kit mutants
(R-HSA-9670439)
Signaling by ptk6
(R-HSA-8848021)
Signaling by raf1 mutants
(R-HSA-9656223)
Signaling by ras mutants
(R-HSA-6802949)
Signaling by receptor tyrosine kinases
(R-HSA-9006934)
Signaling by scf-kit
(R-HSA-1433557)
Signaling by the b cell receptor (bcr)
(R-HSA-983705)
Signaling by type 1 insulin-like growth factor 1 receptor (igf1r)
(R-HSA-2404192)
Signaling by vegf
(R-HSA-194138)
Signal transduction
(R-HSA-162582)
Tie2 signaling
(R-HSA-210993)
Transmission across chemical synapses
(R-HSA-112315)
Vegfa-vegfr2 pathway
(R-HSA-4420097)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 171.5900
Cell Significance Index: -26.6900
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 107.7103
Cell Significance Index: -27.3200
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 58.6077
Cell Significance Index: -27.6700
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 55.0144
Cell Significance Index: -22.3500
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 48.9808
Cell Significance Index: -25.2000
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 23.6975
Cell Significance Index: -22.6300
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 22.2311
Cell Significance Index: -27.4100
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 8.9628
Cell Significance Index: -24.0100
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 7.0324
Cell Significance Index: -27.7500
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 6.3260
Cell Significance Index: -19.4300
Cell Name: oral mucosa squamous cell (CL1001576)
Fold Change: 3.5494
Cell Significance Index: 30.5000
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 3.4476
Cell Significance Index: 93.8400
Cell Name: epidermal cell (CL0000362)
Fold Change: 3.2557
Cell Significance Index: 7.3400
Cell Name: obsolete epithelial cell of alveolus of lung (CL0010003)
Fold Change: 2.8514
Cell Significance Index: 71.1100
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 2.6777
Cell Significance Index: 139.1000
Cell Name: colon goblet cell (CL0009039)
Fold Change: 2.1128
Cell Significance Index: 209.0000
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 2.0740
Cell Significance Index: 337.3200
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: 1.6634
Cell Significance Index: 193.8500
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 1.4686
Cell Significance Index: 180.5800
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 1.4031
Cell Significance Index: 252.9400
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 1.3550
Cell Significance Index: 599.1000
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 1.3482
Cell Significance Index: 95.3500
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 1.1533
Cell Significance Index: 32.2300
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 1.1462
Cell Significance Index: 60.1800
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: 1.0494
Cell Significance Index: 8.8200
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 0.9567
Cell Significance Index: 8.8100
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.8761
Cell Significance Index: 39.7100
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.8358
Cell Significance Index: 52.6800
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.6982
Cell Significance Index: 381.2900
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.6890
Cell Significance Index: 47.6500
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.5498
Cell Significance Index: 75.5000
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.5460
Cell Significance Index: 25.6600
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.5414
Cell Significance Index: 11.7300
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.5338
Cell Significance Index: 24.8900
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.4908
Cell Significance Index: 14.1400
Cell Name: cortical thymic epithelial cell (CL0002364)
Fold Change: 0.4812
Cell Significance Index: 3.9800
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 0.3858
Cell Significance Index: 28.7500
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.3198
Cell Significance Index: 20.6300
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 0.3074
Cell Significance Index: 16.0100
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.2664
Cell Significance Index: 53.4400
Cell Name: lactocyte (CL0002325)
Fold Change: 0.2245
Cell Significance Index: 29.0000
Cell Name: corneal epithelial cell (CL0000575)
Fold Change: 0.2044
Cell Significance Index: 2.9100
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.1460
Cell Significance Index: 52.3800
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1346
Cell Significance Index: 25.6100
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.1274
Cell Significance Index: 25.2900
Cell Name: odontoblast (CL0000060)
Fold Change: 0.1072
Cell Significance Index: 13.7400
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 0.1065
Cell Significance Index: 1.2100
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 0.0753
Cell Significance Index: 2.6200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.0569
Cell Significance Index: 2.0000
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 0.0520
Cell Significance Index: 1.0900
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: 0.0363
Cell Significance Index: 1.8400
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.0341
Cell Significance Index: 0.5700
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0268
Cell Significance Index: 4.5700
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.0227
Cell Significance Index: 16.6700
Cell Name: retinal rod cell (CL0000604)
Fold Change: 0.0210
Cell Significance Index: 0.2500
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.0056
Cell Significance Index: 0.1500
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0054
Cell Significance Index: -4.0500
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: -0.0069
Cell Significance Index: -13.0700
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0088
Cell Significance Index: -16.2900
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0111
Cell Significance Index: -17.1500
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: -0.0158
Cell Significance Index: -10.9300
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0161
Cell Significance Index: -21.8600
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0188
Cell Significance Index: -13.8900
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: -0.0198
Cell Significance Index: -2.3400
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0245
Cell Significance Index: -15.5300
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0293
Cell Significance Index: -16.5100
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0455
Cell Significance Index: -20.6600
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0552
Cell Significance Index: -34.4900
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0587
Cell Significance Index: -6.0000
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.0626
Cell Significance Index: -18.0200
Cell Name: cone retinal bipolar cell (CL0000752)
Fold Change: -0.0740
Cell Significance Index: -0.5700
Cell Name: neuron associated cell (CL0000095)
Fold Change: -0.0971
Cell Significance Index: -3.9800
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.0997
Cell Significance Index: -1.3600
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.1010
Cell Significance Index: -2.1500
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.1125
Cell Significance Index: -16.3500
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1165
Cell Significance Index: -13.3500
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1377
Cell Significance Index: -29.0100
Cell Name: paneth cell of colon (CL0009009)
Fold Change: -0.1535
Cell Significance Index: -2.3000
Cell Name: peg cell (CL4033014)
Fold Change: -0.1643
Cell Significance Index: -3.8000
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.1848
Cell Significance Index: -14.6400
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.1905
Cell Significance Index: -5.0100
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: -0.2340
Cell Significance Index: -1.4400
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.2369
Cell Significance Index: -6.7900
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.2647
Cell Significance Index: -27.5600
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.2826
Cell Significance Index: -21.6900
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.3032
Cell Significance Index: -13.4100
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.3154
Cell Significance Index: -5.4100
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: -0.3385
Cell Significance Index: -3.6800
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.3413
Cell Significance Index: -19.1500
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.4038
Cell Significance Index: -15.2900
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.4249
Cell Significance Index: -13.6100
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.4337
Cell Significance Index: -26.5900
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: -0.5079
Cell Significance Index: -8.9800
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.5145
Cell Significance Index: -11.2700
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.5382
Cell Significance Index: -13.7500
Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
Fold Change: -0.5499
Cell Significance Index: -19.2700
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -0.5519
Cell Significance Index: -18.0700
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.5666
Cell Significance Index: -15.1600
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -0.5705
Cell Significance Index: -18.1700
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -0.5748
Cell Significance Index: -21.1000

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** 1. **GTPase activity**: HRAS is a GTPase, which means it can bind and hydrolyze GTP (guanosine triphosphate), a key molecule in cellular signaling. 2. **Proto-oncogene**: HRAS is a proto-oncogene, which means it has the potential to become an oncogene (cancer-causing gene) if mutated or overexpressed. 3. **Small GTPase**: HRAS is a small GTPase, which distinguishes it from larger GTPases that regulate different cellular processes. 4. **Highly conserved**: The HRAS gene is highly conserved across species, suggesting that it has been crucial for cellular function throughout evolution. **Pathways and Functions** HRAS is involved in various signaling pathways, including: 1. **MAPK pathway**: HRAS activates the MAPK (mitogen-activated protein kinase) pathway, which regulates cell growth, differentiation, and survival. 2. **PI3K/AKT pathway**: HRAS also activates the PI3K/AKT pathway, which regulates cell survival, proliferation, and metabolism. 3. **Raf/MEK/ERK pathway**: HRAS activates the Raf/MEK/ERK pathway, which regulates cell growth, differentiation, and survival. 4. **Akt/PKB pathway**: HRAS activates the Akt/PKB pathway, which regulates cell survival, proliferation, and metabolism. HRAS plays a crucial role in various cellular processes, including: 1. **Cell growth and proliferation**: HRAS regulates cell growth and proliferation by activating the MAPK pathway. 2. **Cell differentiation**: HRAS regulates cell differentiation by activating the PI3K/AKT pathway. 3. **Cell survival**: HRAS regulates cell survival by activating the PI3K/AKT pathway. 4. **Immune responses**: HRAS regulates immune responses by activating the MAPK pathway. **Clinical Significance** Mutations in the HRAS gene have been implicated in various diseases, including: 1. **Cancer**: HRAS mutations are found in many types of cancer, including colorectal, lung, and pancreatic cancer. 2. **Developmental disorders**: HRAS mutations are found in developmental disorders, such as Noonan syndrome and cardiofaciocutaneous syndrome. 3. **Inflammatory conditions**: HRAS mutations are found in inflammatory conditions, such as asthma and autoimmune diseases. 4. **Neurological disorders**: HRAS mutations are found in neurological disorders, such as Parkinson's disease and Alzheimer's disease. In conclusion, the HRAS gene is a critical regulator of cellular signaling pathways, and mutations in this gene have been implicated in various diseases. Further research is needed to fully understand the role of HRAS in human disease and to develop effective therapeutic strategies to target this gene.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

GTPase HRas

Genular Protein ID: 1178990467

Symbol: RASH_HUMAN

Name: GTPase HRas

UniProtKB Accession Codes:

P01112 B5BUA0 Q14080 Q6FHV9 Q9BR65 Q9UCE2

Database IDs:

Citations:

PubMed ID: 6298635

Title: Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue.

PubMed ID: 6298635

DOI: 10.1038/302033a0

PubMed ID: 6844927

Title: Nucleotide sequence analysis of the T24 human bladder carcinoma oncogene.

PubMed ID: 6844927

DOI: 10.1126/science.6844927

PubMed ID: 6087347

Title: Molecular cloning and the total nucleotide sequence of the human c-Ha-ras-1 gene activated in a melanoma from a Japanese patient.

PubMed ID: 6087347

DOI: 10.1073/pnas.81.15.4771

PubMed ID: 14500341

Title: Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus.

PubMed ID: 14500341

PubMed ID: 19054851

Title: Human protein factory for converting the transcriptome into an in vitro-expressed proteome.

PubMed ID: 19054851

DOI: 10.1038/nmeth.1273

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 6290897

Title: Mechanism of activation of a human oncogene.

PubMed ID: 6290897

DOI: 10.1038/300143a0

PubMed ID: 3670300

Title: Identification of the principal promoter sequence of the c-H-ras transforming oncogene: deletion analysis of the 5'-flanking region by focus formation assay.

PubMed ID: 3670300

DOI: 10.1128/mcb.7.8.2933-2940.1987

PubMed ID: 8393791

Title: Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP.

PubMed ID: 8393791

DOI: 10.1111/j.1432-1033.1993.tb18056.x

PubMed ID: 3088563

Title: Isolation of ras GTP-binding mutants using an in situ colony-binding assay.

PubMed ID: 3088563

DOI: 10.1073/pnas.83.13.4607

PubMed ID: 3011420

Title: Deletion mutants of Harvey ras p21 protein reveal the absolute requirement of at least two distant regions for GTP-binding and transforming activities.

PubMed ID: 3011420

DOI: 10.1002/j.1460-2075.1986.tb04267.x

PubMed ID: 2661017

Title: All ras proteins are polyisoprenylated but only some are palmitoylated.

PubMed ID: 2661017

DOI: 10.1016/0092-8674(89)90054-8

PubMed ID: 8626586

Title: Ras, Rap, and Rac small GTP-binding proteins are targets for Clostridium sordellii lethal toxin glucosylation.

PubMed ID: 8626586

DOI: 10.1074/jbc.271.17.10217

PubMed ID: 8626575

Title: Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation.

PubMed ID: 8626575

DOI: 10.1074/jbc.271.17.10149

PubMed ID: 8626715

Title: Palmitoylation of Ha-Ras facilitates membrane binding, activation of downstream effectors, and meiotic maturation in Xenopus oocytes.

PubMed ID: 8626715

DOI: 10.1074/jbc.271.19.11541

PubMed ID: 9020151

Title: A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction.

PubMed ID: 9020151

DOI: 10.1074/jbc.272.7.4323

PubMed ID: 9632667

Title: Functional consequences of monoglucosylation of Ha-Ras at effector domain amino acid threonine 35.

PubMed ID: 9632667

DOI: 10.1074/jbc.273.26.16134

PubMed ID: 10369681

Title: Aiolos transcription factor controls cell death in T cells by regulating Bcl-2 expression and its cellular localization.

PubMed ID: 10369681

DOI: 10.1093/emboj/18.12.3419

PubMed ID: 10608844

Title: RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a Ras/Rap1A-associating domain, is conserved between nematode and humans.

PubMed ID: 10608844

DOI: 10.1074/jbc.274.53.37815

PubMed ID: 11022048

Title: Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras.

PubMed ID: 11022048

DOI: 10.1074/jbc.m008324200

PubMed ID: 11598133

Title: Nedd4 regulates ubiquitination and stability of the guanine-nucleotide exchange factor CNrasGEF.

PubMed ID: 11598133

DOI: 10.1074/jbc.m108373200

PubMed ID: 11257115

Title: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism.

PubMed ID: 11257115

DOI: 10.1083/jcb.152.6.1135

PubMed ID: 11980706

Title: The complex of Arl2-GTP and PDE delta: from structure to function.

PubMed ID: 11980706

DOI: 10.1093/emboj/21.9.2095

PubMed ID: 12684535

Title: The cyclopentenone 15-deoxy-delta 12,14-prostaglandin J2 binds to and activates H-Ras.

PubMed ID: 12684535

DOI: 10.1073/pnas.0735842100

PubMed ID: 22821884

Title: A novel HRAS substitution (c.266C>G; p.S89C) resulting in decreased downstream signaling suggests a new dimension of RAS pathway dysregulation in human development.

PubMed ID: 22821884

DOI: 10.1002/ajmg.a.35449

PubMed ID: 15546861

Title: Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease.

PubMed ID: 15546861

DOI: 10.1074/jbc.m410775200

PubMed ID: 16000296

Title: DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras.

PubMed ID: 16000296

DOI: 10.1074/jbc.m504113200

PubMed ID: 15705808

Title: An acylation cycle regulates localization and activity of palmitoylated Ras isoforms.

PubMed ID: 15705808

DOI: 10.1126/science.1105654

PubMed ID: 17230191

Title: Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin.

PubMed ID: 17230191

DOI: 10.1038/nature05476

PubMed ID: 19744486

Title: Distinct kinetics of (H/K/N)Ras glucosylation and Rac1 glucosylation catalysed by Clostridium sordellii lethal toxin.

PubMed ID: 19744486

DOI: 10.1016/j.febslet.2009.09.006

PubMed ID: 29239724

Title: SIRT2 and lysine fatty acylation regulate the transforming activity of K-Ras4a.

PubMed ID: 29239724

DOI: 10.7554/elife.32436

PubMed ID: 30442762

Title: Mutations in LZTR1 drive human disease by dysregulating RAS ubiquitination.

PubMed ID: 30442762

DOI: 10.1126/science.aap7607

PubMed ID: 2448879

Title: Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21.

PubMed ID: 2448879

DOI: 10.1126/science.2448879

PubMed ID: 2476675

Title: Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation.

PubMed ID: 2476675

DOI: 10.1038/341209a0

PubMed ID: 2196171

Title: Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35-A resolution: implications for the mechanism of GTP hydrolysis.

PubMed ID: 2196171

DOI: 10.1002/j.1460-2075.1990.tb07409.x

PubMed ID: 1899707

Title: Crystal structures at 2.2-A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP.

PubMed ID: 1899707

DOI: 10.1016/0022-2836(91)90753-s

PubMed ID: 8142349

Title: Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.

PubMed ID: 8142349

DOI: 10.1021/bi00178a008

PubMed ID: 9219684

Title: The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants.

PubMed ID: 9219684

DOI: 10.1126/science.277.5324.333

PubMed ID: 10574788

Title: The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins.

PubMed ID: 10574788

DOI: 10.1016/s0969-2126(00)80021-0

PubMed ID: 12213964

Title: The structural basis for the transition from Ras-GTP to Ras-GDP.

PubMed ID: 12213964

DOI: 10.1073/pnas.192453199

PubMed ID: 12740440

Title: Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange.

PubMed ID: 12740440

DOI: 10.1073/pnas.1037299100

PubMed ID: 16698776

Title: A newly designed microspectrofluorometer for kinetic studies on protein crystals in combination with x-ray diffraction.

PubMed ID: 16698776

DOI: 10.1529/biophysj.105.078931

PubMed ID: 18073111

Title: Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf.

PubMed ID: 18073111

DOI: 10.1016/j.str.2007.10.011

PubMed ID: 18596699

Title: Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II.

PubMed ID: 18596699

DOI: 10.1038/emboj.2008.125

PubMed ID: 1459726

Title: The p53 tumor-suppressor gene and ras oncogene mutations in oral squamous-cell carcinoma.

PubMed ID: 1459726

DOI: 10.1002/ijc.2910520606

PubMed ID: 12727991

Title: RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma.

PubMed ID: 12727991

DOI: 10.1210/jc.2002-021907

PubMed ID: 16170316

Title: Germline mutations in HRAS proto-oncogene cause Costello syndrome.

PubMed ID: 16170316

DOI: 10.1038/ng1641

PubMed ID: 16329078

Title: HRAS mutation analysis in Costello syndrome: genotype and phenotype correlation.

PubMed ID: 16329078

DOI: 10.1002/ajmg.a.31047

PubMed ID: 16443854

Title: Genotype-phenotype correlation in Costello syndrome: HRAS mutation analysis in 43 cases.

PubMed ID: 16443854

DOI: 10.1136/jmg.2005.040352

PubMed ID: 17054105

Title: Diversity, parental germline origin, and phenotypic spectrum of de novo HRAS missense changes in Costello syndrome.

PubMed ID: 17054105

DOI: 10.1002/humu.20431

PubMed ID: 17412879

Title: Myopathy caused by HRAS germline mutations: implications for disturbed myogenic differentiation in the presence of constitutive HRas activation.

PubMed ID: 17412879

DOI: 10.1136/jmg.2007.049270

PubMed ID: 18247425

Title: Costello syndrome associated with novel germline HRAS mutations: an attenuated phenotype?

PubMed ID: 18247425

DOI: 10.1002/ajmg.a.32227

PubMed ID: 18039947

Title: Severe neonatal manifestations of Costello syndrome.

PubMed ID: 18039947

DOI: 10.1136/jmg.2007.054411

PubMed ID: 19995790

Title: Duplication of Glu37 in the switch I region of HRAS impairs effector/GAP binding and underlies Costello syndrome by promoting enhanced growth factor-dependent MAPK and AKT activation.

PubMed ID: 19995790

DOI: 10.1093/hmg/ddp548

PubMed ID: 22683711

Title: Postzygotic HRAS and KRAS mutations cause nevus sebaceous and Schimmelpenning syndrome.

PubMed ID: 22683711

DOI: 10.1038/ng.2316

Sequence Information:

Length: 189
Mass: 21298
Checksum: EE6DC2D933E2856A
Sequence:

MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG 
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL 
AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG 
CMSCKCVLS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: HRAS

Associated with

Cells (max top 100)

Other Information

Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue. PubMed ID: 6298635

Nucleotide sequence analysis of the T24 human bladder carcinoma oncogene. PubMed ID: 6844927

Molecular cloning and the total nucleotide sequence of the human c-Ha-ras-1 gene activated in a melanoma from a Japanese patient. PubMed ID: 6087347

Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus. PubMed ID: 14500341

Human protein factory for converting the transcriptome into an in vitro-expressed proteome. PubMed ID: 19054851

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Mechanism of activation of a human oncogene. PubMed ID: 6290897

Identification of the principal promoter sequence of the c-H-ras transforming oncogene: deletion analysis of the 5'-flanking region by focus formation assay. PubMed ID: 3670300

Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP. PubMed ID: 8393791

Isolation of ras GTP-binding mutants using an in situ colony-binding assay. PubMed ID: 3088563

Deletion mutants of Harvey ras p21 protein reveal the absolute requirement of at least two distant regions for GTP-binding and transforming activities. PubMed ID: 3011420

All ras proteins are polyisoprenylated but only some are palmitoylated. PubMed ID: 2661017

Ras, Rap, and Rac small GTP-binding proteins are targets for Clostridium sordellii lethal toxin glucosylation. PubMed ID: 8626586

Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation. PubMed ID: 8626575

Palmitoylation of Ha-Ras facilitates membrane binding, activation of downstream effectors, and meiotic maturation in Xenopus oocytes. PubMed ID: 8626715

A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction. PubMed ID: 9020151

Functional consequences of monoglucosylation of Ha-Ras at effector domain amino acid threonine 35. PubMed ID: 9632667

Aiolos transcription factor controls cell death in T cells by regulating Bcl-2 expression and its cellular localization. PubMed ID: 10369681

RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a Ras/Rap1A-associating domain, is conserved between nematode and humans. PubMed ID: 10608844

Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. PubMed ID: 11022048

Nedd4 regulates ubiquitination and stability of the guanine-nucleotide exchange factor CNrasGEF. PubMed ID: 11598133

Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. PubMed ID: 11257115

The complex of Arl2-GTP and PDE delta: from structure to function. PubMed ID: 11980706

The cyclopentenone 15-deoxy-delta 12,14-prostaglandin J2 binds to and activates H-Ras. PubMed ID: 12684535

A novel HRAS substitution (c.266C&gt;G; p.S89C) resulting in decreased downstream signaling suggests a new dimension of RAS pathway dysregulation in human development. PubMed ID: 22821884

Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease. PubMed ID: 15546861

DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. PubMed ID: 16000296

An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. PubMed ID: 15705808

Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin. PubMed ID: 17230191

Distinct kinetics of (H/K/N)Ras glucosylation and Rac1 glucosylation catalysed by Clostridium sordellii lethal toxin. PubMed ID: 19744486

SIRT2 and lysine fatty acylation regulate the transforming activity of K-Ras4a. PubMed ID: 29239724

Mutations in LZTR1 drive human disease by dysregulating RAS ubiquitination. PubMed ID: 30442762

Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21. PubMed ID: 2448879

Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. PubMed ID: 2476675

Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35-A resolution: implications for the mechanism of GTP hydrolysis. PubMed ID: 2196171

Crystal structures at 2.2-A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. PubMed ID: 1899707

Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. PubMed ID: 8142349

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. PubMed ID: 9219684

The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins. PubMed ID: 10574788

The structural basis for the transition from Ras-GTP to Ras-GDP. PubMed ID: 12213964

Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange. PubMed ID: 12740440

A newly designed microspectrofluorometer for kinetic studies on protein crystals in combination with x-ray diffraction. PubMed ID: 16698776

Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf. PubMed ID: 18073111

Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II. PubMed ID: 18596699

The p53 tumor-suppressor gene and ras oncogene mutations in oral squamous-cell carcinoma. PubMed ID: 1459726

RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma. PubMed ID: 12727991

Germline mutations in HRAS proto-oncogene cause Costello syndrome. PubMed ID: 16170316

HRAS mutation analysis in Costello syndrome: genotype and phenotype correlation. PubMed ID: 16329078

Genotype-phenotype correlation in Costello syndrome: HRAS mutation analysis in 43 cases. PubMed ID: 16443854

Diversity, parental germline origin, and phenotypic spectrum of de novo HRAS missense changes in Costello syndrome. PubMed ID: 17054105

Myopathy caused by HRAS germline mutations: implications for disturbed myogenic differentiation in the presence of constitutive HRas activation. PubMed ID: 17412879

Costello syndrome associated with novel germline HRAS mutations: an attenuated phenotype? PubMed ID: 18247425

Severe neonatal manifestations of Costello syndrome. PubMed ID: 18039947

Duplication of Glu37 in the switch I region of HRAS impairs effector/GAP binding and underlies Costello syndrome by promoting enhanced growth factor-dependent MAPK and AKT activation. PubMed ID: 19995790

Postzygotic HRAS and KRAS mutations cause nevus sebaceous and Schimmelpenning syndrome. PubMed ID: 22683711