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Protein

GTPase HRas

Gene

HRAS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.3 Publications

Enzyme regulationi

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).

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 17GTP8
Nucleotide bindingi57 – 61GTP5
Nucleotide bindingi116 – 119GTP4

GO - Molecular functioni

  • GTPase activity Source: WormBase
  • GTP binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB

GO - Biological processi

  • animal organ morphogenesis Source: ProtInc
  • axon guidance Source: Reactome
  • cell cycle arrest Source: BHF-UCL
  • cell proliferation Source: Ensembl
  • cell surface receptor signaling pathway Source: ProtInc
  • cellular senescence Source: BHF-UCL
  • chemotaxis Source: ProtInc
  • defense response to protozoan Source: Ensembl
  • endocytosis Source: Ensembl
  • ephrin receptor signaling pathway Source: Reactome
  • epidermal growth factor receptor signaling pathway Source: Reactome
  • ERBB2 signaling pathway Source: Reactome
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • intrinsic apoptotic signaling pathway Source: Ensembl
  • leukocyte migration Source: Reactome
  • MAPK cascade Source: Reactome
  • mitotic cell cycle checkpoint Source: BHF-UCL
  • negative regulation of cell 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 proliferation Source: BHF-UCL
  • positive regulation of DNA replication 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 protein phosphorylation Source: BHF-UCL
  • positive regulation of Ras protein signal transduction Source: Ensembl
  • positive regulation of ruffle assembly Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of wound healing Source: BHF-UCL
  • protein heterooligomerization Source: Ensembl
  • Ras protein signal transduction Source: BHF-UCL
  • regulation of long-term neuronal synaptic plasticity Source: Ensembl
  • signal transduction Source: ProtInc
  • social behavior Source: Ensembl
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • T cell receptor signaling pathway Source: Ensembl
  • T-helper 1 type immune response Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000174775-MONOMER.
ReactomeiR-HSA-112412. SOS-mediated signalling.
R-HSA-1169092. Activation of RAS in B cells.
R-HSA-1236382. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
R-HSA-1250196. SHC1 events in ERBB2 signaling.
R-HSA-1250347. SHC1 events in ERBB4 signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-167044. Signalling to RAS.
R-HSA-171007. p38MAPK events.
R-HSA-179812. GRB2 events in EGFR signaling.
R-HSA-180336. SHC1 events in EGFR signaling.
R-HSA-186763. Downstream signal transduction.
R-HSA-1963640. GRB2 events in ERBB2 signaling.
R-HSA-210993. Tie2 Signaling.
R-HSA-2179392. EGFR Transactivation by Gastrin.
R-HSA-2424491. DAP12 signaling.
R-HSA-2428933. SHC-related events triggered by IGF1R.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-5637810. Constitutive Signaling by EGFRvIII.
R-HSA-5654688. SHC-mediated cascade:FGFR1.
R-HSA-5654693. FRS-mediated FGFR1 signaling.
R-HSA-5654699. SHC-mediated cascade:FGFR2.
R-HSA-5654700. FRS-mediated FGFR2 signaling.
R-HSA-5654704. SHC-mediated cascade:FGFR3.
R-HSA-5654706. FRS-mediated FGFR3 signaling.
R-HSA-5654712. FRS-mediated FGFR4 signaling.
R-HSA-5654719. SHC-mediated cascade:FGFR4.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5655291. Signaling by FGFR4 in disease.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5673000. RAF activation.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802953. RAS signaling downstream of NF1 loss-of-function variants.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
R-HSA-74751. Insulin receptor signalling cascade.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
R-HSA-8851805. MET activates RAS signaling.
R-HSA-8853334. Signaling by FGFR3 fusions in cancer.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
SignaLinkiP01112.
SIGNORiP01112.

Names & Taxonomyi

Protein namesi
Recommended name:
GTPase HRas
Alternative name(s):
H-Ras-1
Ha-Ras
Transforming protein p21
c-H-ras
p21ras
Cleaved into the following chain:
Gene namesi
Name:HRAS
Synonyms:HRAS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:5173. HRAS.

Subcellular locationi

Isoform 2 :

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Costello syndrome (CSTLO)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:218040
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02610612G → A in CSTLO. 3 PublicationsCorresponds to variant rs104894230dbSNPEnsembl.1
Natural variantiVAR_04597512G → C in CSTLO. 2 PublicationsCorresponds to variant rs104894229dbSNPEnsembl.1
Natural variantiVAR_06881612G → D in CSTLO; severe mutation. 1 PublicationCorresponds to variant rs104894230dbSNPEnsembl.1
Natural variantiVAR_04597612G → E in CSTLO. 1 Publication1
Natural variantiVAR_00683712G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant rs104894229dbSNPEnsembl.1
Natural variantiVAR_00683612G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane; loss of interaction with and recruitment to plasma membrane of PLCE1 when associated with F-32; loss of interaction with PLCE1 when associated with G-26, F-32 and S-35; no effect on interaction with PLCE1 when associated with A-29, G-34, G-37, N-38 and C-39; no effect on subcellular location of isoform 2. 4 PublicationsCorresponds to variant rs104894230dbSNPEnsembl.1
Natural variantiVAR_02610713G → C in CSTLO. 1 PublicationCorresponds to variant rs104894228dbSNPEnsembl.1
Natural variantiVAR_02610813G → D in CSTLO. 1 PublicationCorresponds to variant rs104894226dbSNPEnsembl.1
Natural variantiVAR_06881837E → EE in CSTLO. 1 Publication1
Natural variantiVAR_04597858T → I in CSTLO. 1 PublicationCorresponds to variant rs121917758dbSNPEnsembl.1
Natural variantiVAR_045981117K → R in CSTLO. 1 PublicationCorresponds to variant rs104894227dbSNPEnsembl.1
Natural variantiVAR_045982146A → T in CSTLO. 1 PublicationCorresponds to variant rs104894231dbSNPEnsembl.1
Natural variantiVAR_045983146A → V in CSTLO. 1 PublicationCorresponds to variant rs121917759dbSNPEnsembl.1
Congenital myopathy with excess of muscle spindles (CMEMS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionVariant of Costello syndrome.
See also OMIM:218040
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00683712G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant rs104894229dbSNPEnsembl.1
Natural variantiVAR_00683612G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane; loss of interaction with and recruitment to plasma membrane of PLCE1 when associated with F-32; loss of interaction with PLCE1 when associated with G-26, F-32 and S-35; no effect on interaction with PLCE1 when associated with A-29, G-34, G-37, N-38 and C-39; no effect on subcellular location of isoform 2. 4 PublicationsCorresponds to variant rs104894230dbSNPEnsembl.1
Natural variantiVAR_04597722Q → K in CMEMS. 1 PublicationCorresponds to variant rs121917757dbSNPEnsembl.1
Natural variantiVAR_04598063E → K in CMEMS. 1 PublicationCorresponds to variant rs121917756dbSNPEnsembl.1
Thyroid cancer, non-medullary, 2 (NMTC2)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:188470
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04597961Q → K in NMTC2; somatic mutation; increases transformation of cultured cell lines. 2 PublicationsCorresponds to variant rs28933406dbSNPEnsembl.1

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)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:109800
Schimmelpenning-Feuerstein-Mims syndrome (SFM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:163200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06881713G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. 1 PublicationCorresponds to variant rs104894228dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17S → N: Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2. 2 Publications1
Mutagenesisi26N → G: Loss of interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi29V → A: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi32Y → F: Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi34P → G: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi35T → S: Loss of interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi37E → G: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi38D → N: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi39S → C: No effect on interaction with PLCE1; when associated with V-12. 1 Publication1
Mutagenesisi59A → T: Loss of GTPase activity and creation of an autophosphorylation site. 1
Mutagenesisi61Q → I: Moderately increased transformation of cultured cell lines. 1 Publication1
Mutagenesisi61Q → V: Strongly increased transformation of cultured cell lines. 1 Publication1
Mutagenesisi83A → T: GTP-binding activity reduced by factor of 30. 1 Publication1
Mutagenesisi118C → S: Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange. 2 Publications1
Mutagenesisi119D → N: Loss of GTP-binding activity. 1 Publication1
Mutagenesisi144T → I: GTP-binding activity reduced by factor of 25. 1 Publication1
Mutagenesisi164 – 165RQ → AV: Loss of GTP-binding activity. 1 Publication2
Mutagenesisi181C → S: Exclusively localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-184. 2 Publications1
Mutagenesisi184C → 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. 3 Publications1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNETi3265.
MalaCardsiHRAS.
MIMi109800. phenotype.
163200. phenotype.
188470. phenotype.
218040. phenotype.
OpenTargetsiENSG00000174775.
ENSG00000276536.
Orphaneti3071. Costello syndrome.
2612. Linear nevus sebaceus syndrome.
2874. Phakomatosis pigmentokeratotica.
PharmGKBiPA29444.

Chemistry databases

ChEMBLiCHEMBL2167.
GuidetoPHARMACOLOGYi2822.

Polymorphism and mutation databases

BioMutaiHRAS.
DMDMi131869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000429961 – 186GTPase HRasAdd BLAST186
Initiator methionineiRemoved; alternate1 Publication
ChainiPRO_00003264762 – 186GTPase HRas, N-terminally processedAdd BLAST185
PropeptideiPRO_0000042997187 – 189Removed in mature form3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine; in GTPase HRas; alternate1 Publication1
Modified residuei2N-acetylthreonine; in GTPase HRas, N-terminally processed1 Publication1
Modified residuei118S-nitrosocysteine1 Publication1
Lipidationi181S-palmitoyl cysteine4 Publications1
Lipidationi184S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate1 Publication1
Lipidationi184S-palmitoyl cysteine; alternate4 Publications1
Modified residuei186Cysteine methyl ester1 Publication1
Lipidationi186S-farnesyl cysteine1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Palmitate, Prenylation, S-nitrosylation

Proteomic databases

EPDiP01112.
PaxDbiP01112.
PeptideAtlasiP01112.
PRIDEiP01112.

PTM databases

iPTMnetiP01112.
PhosphoSitePlusiP01112.
SwissPalmiP01112.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000174775.
CleanExiHS_HRAS.
ExpressionAtlasiP01112. baseline and differential.
GenevisibleiP01112. HS.

Organism-specific databases

HPAiCAB002015.
HPA049830.

Interactioni

Subunit structurei

In its GTP-bound form interacts with PLCE1 (PubMed:11022048). Interacts with TBC1D10C (PubMed:17230191). Interacts with RGL3 (By similarity). Interacts with HSPD1 (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (By similarity). Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) (By similarity). Forms a signaling complex with RASGRP1 and DGKZ (PubMed:11257115). Interacts with RASSF5 (PubMed:18596699). Interacts with PDE6D (PubMed:11980706). Interacts with IKZF3 (PubMed:10369681). Interacts with RACK1 (PubMed:14500341). Interacts with PIK3CG; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (By similarity). Interacts with RAPGEF2 (PubMed:10608844, PubMed:11598133).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRAPQ7Z5693EBI-350145,EBI-349900
Pik3caP423372EBI-350145,EBI-641748From a different organism.
PIK3CDO003292EBI-350145,EBI-718309
PIK3CDO00329-22EBI-350145,EBI-6470902
Rabac1Q9Z0S94EBI-350145,EBI-476965From a different organism.
RAF1P0404914EBI-350145,EBI-365996
RALGDSQ129672EBI-350145,EBI-365861
Rapgef4Q9EQZ63EBI-350145,EBI-772212From a different organism.
RASSF1Q9NS23-22EBI-350145,EBI-438698
RASSF5Q8WWW02EBI-350145,EBI-367390
Rassf5Q5EBH111EBI-350145,EBI-960530From a different organism.
Rassf5Q5EBH1-23EBI-350145,EBI-960547From a different organism.
RIN1Q136715EBI-350145,EBI-366017
SOS1Q078898EBI-350145,EBI-297487

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109501. 91 interactors.
DIPiDIP-1050N.
IntActiP01112. 49 interactors.
MINTiMINT-5002362.
STRINGi9606.ENSP00000309845.

Chemistry databases

BindingDBiP01112.

Structurei

Secondary structure

1189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Beta strandi12 – 14Combined sources3
Helixi16 – 25Combined sources10
Beta strandi27 – 31Combined sources5
Beta strandi34 – 37Combined sources4
Beta strandi38 – 46Combined sources9
Beta strandi49 – 57Combined sources9
Beta strandi60 – 63Combined sources4
Helixi66 – 74Combined sources9
Beta strandi76 – 83Combined sources8
Turni84 – 86Combined sources3
Helixi87 – 104Combined sources18
Beta strandi105 – 107Combined sources3
Beta strandi111 – 116Combined sources6
Beta strandi120 – 122Combined sources3
Helixi127 – 136Combined sources10
Beta strandi141 – 144Combined sources4
Turni146 – 148Combined sources3
Helixi152 – 164Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
121PX-ray1.54A1-166[»]
1AA9NMR-A1-171[»]
1AGPX-ray2.30A1-166[»]
1BKDX-ray2.80R1-166[»]
1CLUX-ray1.70A1-166[»]
1CRPNMR-A1-166[»]
1CRQNMR-A1-166[»]
1CRRNMR-A1-166[»]
1CTQX-ray1.26A1-166[»]
1GNPX-ray2.70A1-166[»]
1GNQX-ray2.50A1-166[»]
1GNRX-ray1.85A1-166[»]
1HE8X-ray3.00B1-166[»]
1IAQX-ray2.90A/B/C1-166[»]
1IOZX-ray2.00A1-171[»]
1JAHX-ray1.80A1-166[»]
1JAIX-ray1.80A1-166[»]
1K8RX-ray3.00A1-166[»]
1LF0X-ray1.70A1-166[»]
1LF5X-ray1.70A1-166[»]
1LFDX-ray2.10B/D1-167[»]
1NVUX-ray2.20Q/R1-166[»]
1NVVX-ray2.18Q/R1-166[»]
1NVWX-ray2.70Q/R1-166[»]
1NVXX-ray3.20Q/R1-166[»]
1P2SX-ray2.45A1-166[»]
1P2TX-ray2.00A1-166[»]
1P2UX-ray2.00A1-166[»]
1P2VX-ray2.30A1-166[»]
1PLJX-ray2.80A1-166[»]
1PLKX-ray2.80A1-166[»]
1PLLX-ray2.80A1-166[»]
1Q21X-ray2.20A1-171[»]
1QRAX-ray1.60A1-166[»]
1RVDX-ray1.90A1-166[»]
1WQ1X-ray2.50R1-166[»]
1XCMX-ray1.84A1-167[»]
1XD2X-ray2.70A/B1-166[»]
1XJ0X-ray1.70A1-166[»]
1ZVQX-ray2.00A1-166[»]
1ZW6X-ray1.50A1-166[»]
221PX-ray2.30A1-166[»]
2C5LX-ray1.90A/B1-166[»]
2CE2X-ray1.00X1-166[»]
2CL0X-ray1.80X1-166[»]
2CL6X-ray1.24X1-166[»]
2CL7X-ray1.25X1-166[»]
2CLCX-ray1.30X1-166[»]
2CLDX-ray1.22X1-166[»]
2EVWX-ray1.05X1-166[»]
2GDPmodel-A1-171[»]
2LCFNMR-A1-166[»]
2LWINMR-A1-166[»]
2N42NMR-A1-166[»]
2N46NMR-A1-166[»]
2Q21X-ray2.20A1-171[»]
2QUZX-ray1.49A1-166[»]
2RGAX-ray1.90A1-166[»]
2RGBX-ray1.35A1-166[»]
2RGCX-ray1.60A1-166[»]
2RGDX-ray2.00A1-166[»]
2RGEX-ray1.40A1-166[»]
2RGGX-ray1.45A1-166[»]
2UZIX-ray2.00R1-166[»]
2VH5X-ray2.70R1-166[»]
2X1VX-ray1.70A1-166[»]
3DDCX-ray1.80A1-166[»]
3I3SX-ray1.36R1-166[»]
3K8YX-ray1.30A1-166[»]
3K9LX-ray1.80A/B/C1-166[»]
3K9NX-ray2.00A1-166[»]
3KKMX-ray1.70A1-166[»]
3KKNX-ray2.09A1-166[»]
3KUDX-ray2.15A1-166[»]
3L8YX-ray2.02A1-166[»]
3L8ZX-ray1.44A1-166[»]
3LBHX-ray1.85A1-166[»]
3LBIX-ray2.09A1-166[»]
3LBNX-ray1.86A1-166[»]
3LO5X-ray2.57A/C/E1-166[»]
3OIUX-ray1.32A1-166[»]
3OIVX-ray1.84A1-166[»]
3OIWX-ray1.30A1-166[»]
3RRYX-ray1.60A1-166[»]
3RRZX-ray1.60A1-166[»]
3RS0X-ray1.40A1-166[»]
3RS2X-ray1.84A1-166[»]
3RS3X-ray1.52A1-166[»]
3RS4X-ray1.70A1-166[»]
3RS5X-ray1.68A1-166[»]
3RS7X-ray1.70A1-166[»]
3RSLX-ray1.70A1-166[»]
3RSOX-ray1.60A1-166[»]
3TGPX-ray1.31A1-166[»]
421PX-ray2.20A1-166[»]
4DLRX-ray1.32A1-166[»]
4DLSX-ray1.82A1-166[»]
4DLTX-ray1.70A1-166[»]
4DLUX-ray1.60A1-166[»]
4DLVX-ray1.57A1-166[»]
4DLWX-ray1.72A1-166[»]
4DLXX-ray1.73A1-166[»]
4DLYX-ray1.57A1-166[»]
4DLZX-ray1.66A1-166[»]
4DSTX-ray2.30A2-167[»]
4DSUX-ray1.70A2-167[»]
4EFLX-ray1.90A1-166[»]
4EFMX-ray1.90A1-166[»]
4EFNX-ray2.30A1-166[»]
4G0NX-ray2.45A1-166[»]
4G3XX-ray3.25A1-166[»]
4K81X-ray2.40B/D/F/H1-166[»]
4L9SX-ray1.61A1-166[»]
4L9WX-ray1.95A1-166[»]
4NYIX-ray2.96Q/R1-166[»]
4NYJX-ray2.85Q/R1-166[»]
4NYMX-ray3.55Q/R1-166[»]
4Q21X-ray2.00A1-189[»]
4RSGneutron diffraction1.91A1-166[»]
4URUX-ray2.83R1-166[»]
4URVX-ray2.58R1-166[»]
4URWX-ray2.76R1-166[»]
4URXX-ray2.49R1-166[»]
4URYX-ray2.47R1-166[»]
4URZX-ray2.24R1-166[»]
4US0X-ray2.17R1-166[»]
4US1X-ray2.65R1-166[»]
4US2X-ray2.48R1-166[»]
4XVQX-ray1.89A1-166[»]
4XVRX-ray2.03A1-166[»]
521PX-ray2.60A1-166[»]
5B2ZX-ray1.56A1-166[»]
5B30X-ray1.60A1-166[»]
5P21X-ray1.35A1-166[»]
621PX-ray2.40A1-166[»]
6Q21X-ray1.95A/B/C/D1-171[»]
721PX-ray2.00A1-166[»]
821PX-ray1.50A1-166[»]
DisProtiDP00153.
ProteinModelPortaliP01112.
SMRiP01112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01112.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni166 – 185Hypervariable regionAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi32 – 40Effector region9

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00860000133672.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP01112.
KOiK02833.
OMAiDCMNCKC.
OrthoDBiEOG091G0UAU.
PhylomeDBiP01112.
TreeFamiTF312796.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P01112-1) [UniParc]FASTAAdd to basket
Also known as: H-Ras4A, p21

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET
60 70 80 90 100
CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI
110 120 130 140 150
KRVKDSDDVP MVLVGNKCDL AARTVESRQA QDLARSYGIP YIETSAKTRQ
160 170 180
GVEDAFYTLV REIRQHKLRK LNPPDESGPG CMSCKCVLS
Length:189
Mass (Da):21,298
Last modified:July 21, 1986 - v1
Checksum:iEE6DC2D933E2856A
GO
Isoform 2 (identifier: P01112-2) [UniParc]FASTAAdd to basket
Also known as: H-RasIDX, p19

The sequence of this isoform differs from the canonical sequence as follows:
     152-189: VEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS → SRSGSSSSSGTLWDPPGPM

Show »
Length:170
Mass (Da):18,870
Checksum:iC3364C8DC783C191
GO

Mass spectrometryi

Molecular mass is 6223±2 Da from positions 112 - 166. Determined by ESI. 1 Publication
Molecular mass is 6253±2 Da from positions 112 - 166. Determined by ESI. Includes one nitric oxide molecule.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02610612G → A in CSTLO. 3 PublicationsCorresponds to variant rs104894230dbSNPEnsembl.1
Natural variantiVAR_04597512G → C in CSTLO. 2 PublicationsCorresponds to variant rs104894229dbSNPEnsembl.1
Natural variantiVAR_06881612G → D in CSTLO; severe mutation. 1 PublicationCorresponds to variant rs104894230dbSNPEnsembl.1
Natural variantiVAR_04597612G → E in CSTLO. 1 Publication1
Natural variantiVAR_00683712G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant rs104894229dbSNPEnsembl.1
Natural variantiVAR_00683612G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane; loss of interaction with and recruitment to plasma membrane of PLCE1 when associated with F-32; loss of interaction with PLCE1 when associated with G-26, F-32 and S-35; no effect on interaction with PLCE1 when associated with A-29, G-34, G-37, N-38 and C-39; no effect on subcellular location of isoform 2. 4 PublicationsCorresponds to variant rs104894230dbSNPEnsembl.1
Natural variantiVAR_02610713G → C in CSTLO. 1 PublicationCorresponds to variant rs104894228dbSNPEnsembl.1
Natural variantiVAR_02610813G → D in CSTLO. 1 PublicationCorresponds to variant rs104894226dbSNPEnsembl.1
Natural variantiVAR_06881713G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. 1 PublicationCorresponds to variant rs104894228dbSNPEnsembl.1
Natural variantiVAR_04597722Q → K in CMEMS. 1 PublicationCorresponds to variant rs121917757dbSNPEnsembl.1
Natural variantiVAR_06881837E → EE in CSTLO. 1 Publication1
Natural variantiVAR_04597858T → I in CSTLO. 1 PublicationCorresponds to variant rs121917758dbSNPEnsembl.1
Natural variantiVAR_04597961Q → K in NMTC2; somatic mutation; increases transformation of cultured cell lines. 2 PublicationsCorresponds to variant rs28933406dbSNPEnsembl.1
Natural variantiVAR_00683861Q → L in melanoma; strongly reduced GTP hydrolysis in the presence of RAF1; increases transformation of cultured cell lines. 1 PublicationCorresponds to variant rs121913233dbSNPEnsembl.1
Natural variantiVAR_04598063E → K in CMEMS. 1 PublicationCorresponds to variant rs121917756dbSNPEnsembl.1
Natural variantiVAR_045981117K → R in CSTLO. 1 PublicationCorresponds to variant rs104894227dbSNPEnsembl.1
Natural variantiVAR_045982146A → T in CSTLO. 1 PublicationCorresponds to variant rs104894231dbSNPEnsembl.1
Natural variantiVAR_045983146A → V in CSTLO. 1 PublicationCorresponds to variant rs121917759dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_041597152 – 189VEDAF…KCVLS → SRSGSSSSSGTLWDPPGPM in isoform 2. 2 PublicationsAdd BLAST38

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00277 Genomic DNA. Translation: AAB02605.1.
AJ437024 mRNA. Translation: CAD24594.1.
AF493916 mRNA. Translation: AAM12630.1.
CR536579 mRNA. Translation: CAG38816.1.
CR542271 mRNA. Translation: CAG47067.1.
BT019421 mRNA. Translation: AAV38228.1.
EF015887 Genomic DNA. Translation: ABI97389.1.
AB451336 mRNA. Translation: BAG70150.1.
AB451485 mRNA. Translation: BAG70299.1.
CH471158 Genomic DNA. Translation: EAX02337.1.
CH471158 Genomic DNA. Translation: EAX02338.1.
BC006499 mRNA. Translation: AAH06499.1.
BC095471 mRNA. Translation: AAH95471.1.
M17232 Genomic DNA. Translation: AAA35685.1.
CCDSiCCDS7698.1. [P01112-1]
CCDS7699.1. [P01112-2]
PIRiA93299. TVHUH.
RefSeqiNP_001123914.1. NM_001130442.2. [P01112-1]
NP_001304983.1. NM_001318054.1.
NP_005334.1. NM_005343.3. [P01112-1]
NP_789765.1. NM_176795.4. [P01112-2]
UniGeneiHs.37003.

Genome annotation databases

EnsembliENST00000311189; ENSP00000309845; ENSG00000174775. [P01112-1]
ENST00000397594; ENSP00000380722; ENSG00000174775. [P01112-2]
ENST00000397596; ENSP00000380723; ENSG00000174775. [P01112-1]
ENST00000417302; ENSP00000388246; ENSG00000174775. [P01112-2]
ENST00000451590; ENSP00000407586; ENSG00000174775. [P01112-1]
ENST00000493230; ENSP00000434023; ENSG00000174775. [P01112-2]
ENST00000610977; ENSP00000480686; ENSG00000276536. [P01112-1]
ENST00000615062; ENSP00000482366; ENSG00000276536. [P01112-1]
ENST00000616241; ENSP00000480317; ENSG00000276536. [P01112-2]
ENST00000631404; ENSP00000488757; ENSG00000276536. [P01112-1]
ENST00000631967; ENSP00000488225; ENSG00000276536. [P01112-2]
ENST00000634098; ENSP00000488296; ENSG00000276536. [P01112-2]
GeneIDi3265.
KEGGihsa:3265.
UCSCiuc010qvw.3. human. [P01112-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00277 Genomic DNA. Translation: AAB02605.1.
AJ437024 mRNA. Translation: CAD24594.1.
AF493916 mRNA. Translation: AAM12630.1.
CR536579 mRNA. Translation: CAG38816.1.
CR542271 mRNA. Translation: CAG47067.1.
BT019421 mRNA. Translation: AAV38228.1.
EF015887 Genomic DNA. Translation: ABI97389.1.
AB451336 mRNA. Translation: BAG70150.1.
AB451485 mRNA. Translation: BAG70299.1.
CH471158 Genomic DNA. Translation: EAX02337.1.
CH471158 Genomic DNA. Translation: EAX02338.1.
BC006499 mRNA. Translation: AAH06499.1.
BC095471 mRNA. Translation: AAH95471.1.
M17232 Genomic DNA. Translation: AAA35685.1.
CCDSiCCDS7698.1. [P01112-1]
CCDS7699.1. [P01112-2]
PIRiA93299. TVHUH.
RefSeqiNP_001123914.1. NM_001130442.2. [P01112-1]
NP_001304983.1. NM_001318054.1.
NP_005334.1. NM_005343.3. [P01112-1]
NP_789765.1. NM_176795.4. [P01112-2]
UniGeneiHs.37003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
121PX-ray1.54A1-166[»]
1AA9NMR-A1-171[»]
1AGPX-ray2.30A1-166[»]
1BKDX-ray2.80R1-166[»]
1CLUX-ray1.70A1-166[»]
1CRPNMR-A1-166[»]
1CRQNMR-A1-166[»]
1CRRNMR-A1-166[»]
1CTQX-ray1.26A1-166[»]
1GNPX-ray2.70A1-166[»]
1GNQX-ray2.50A1-166[»]
1GNRX-ray1.85A1-166[»]
1HE8X-ray3.00B1-166[»]
1IAQX-ray2.90A/B/C1-166[»]
1IOZX-ray2.00A1-171[»]
1JAHX-ray1.80A1-166[»]
1JAIX-ray1.80A1-166[»]
1K8RX-ray3.00A1-166[»]
1LF0X-ray1.70A1-166[»]
1LF5X-ray1.70A1-166[»]
1LFDX-ray2.10B/D1-167[»]
1NVUX-ray2.20Q/R1-166[»]
1NVVX-ray2.18Q/R1-166[»]
1NVWX-ray2.70Q/R1-166[»]
1NVXX-ray3.20Q/R1-166[»]
1P2SX-ray2.45A1-166[»]
1P2TX-ray2.00A1-166[»]
1P2UX-ray2.00A1-166[»]
1P2VX-ray2.30A1-166[»]
1PLJX-ray2.80A1-166[»]
1PLKX-ray2.80A1-166[»]
1PLLX-ray2.80A1-166[»]
1Q21X-ray2.20A1-171[»]
1QRAX-ray1.60A1-166[»]
1RVDX-ray1.90A1-166[»]
1WQ1X-ray2.50R1-166[»]
1XCMX-ray1.84A1-167[»]
1XD2X-ray2.70A/B1-166[»]
1XJ0X-ray1.70A1-166[»]
1ZVQX-ray2.00A1-166[»]
1ZW6X-ray1.50A1-166[»]
221PX-ray2.30A1-166[»]
2C5LX-ray1.90A/B1-166[»]
2CE2X-ray1.00X1-166[»]
2CL0X-ray1.80X1-166[»]
2CL6X-ray1.24X1-166[»]
2CL7X-ray1.25X1-166[»]
2CLCX-ray1.30X1-166[»]
2CLDX-ray1.22X1-166[»]
2EVWX-ray1.05X1-166[»]
2GDPmodel-A1-171[»]
2LCFNMR-A1-166[»]
2LWINMR-A1-166[»]
2N42NMR-A1-166[»]
2N46NMR-A1-166[»]
2Q21X-ray2.20A1-171[»]
2QUZX-ray1.49A1-166[»]
2RGAX-ray1.90A1-166[»]
2RGBX-ray1.35A1-166[»]
2RGCX-ray1.60A1-166[»]
2RGDX-ray2.00A1-166[»]
2RGEX-ray1.40A1-166[»]
2RGGX-ray1.45A1-166[»]
2UZIX-ray2.00R1-166[»]
2VH5X-ray2.70R1-166[»]
2X1VX-ray1.70A1-166[»]
3DDCX-ray1.80A1-166[»]
3I3SX-ray1.36R1-166[»]
3K8YX-ray1.30A1-166[»]
3K9LX-ray1.80A/B/C1-166[»]
3K9NX-ray2.00A1-166[»]
3KKMX-ray1.70A1-166[»]
3KKNX-ray2.09A1-166[»]
3KUDX-ray2.15A1-166[»]
3L8YX-ray2.02A1-166[»]
3L8ZX-ray1.44A1-166[»]
3LBHX-ray1.85A1-166[»]
3LBIX-ray2.09A1-166[»]
3LBNX-ray1.86A1-166[»]
3LO5X-ray2.57A/C/E1-166[»]
3OIUX-ray1.32A1-166[»]
3OIVX-ray1.84A1-166[»]
3OIWX-ray1.30A1-166[»]
3RRYX-ray1.60A1-166[»]
3RRZX-ray1.60A1-166[»]
3RS0X-ray1.40A1-166[»]
3RS2X-ray1.84A1-166[»]
3RS3X-ray1.52A1-166[»]
3RS4X-ray1.70A1-166[»]
3RS5X-ray1.68A1-166[»]
3RS7X-ray1.70A1-166[»]
3RSLX-ray1.70A1-166[»]
3RSOX-ray1.60A1-166[»]
3TGPX-ray1.31A1-166[»]
421PX-ray2.20A1-166[»]
4DLRX-ray1.32A1-166[»]
4DLSX-ray1.82A1-166[»]
4DLTX-ray1.70A1-166[»]
4DLUX-ray1.60A1-166[»]
4DLVX-ray1.57A1-166[»]
4DLWX-ray1.72A1-166[»]
4DLXX-ray1.73A1-166[»]
4DLYX-ray1.57A1-166[»]
4DLZX-ray1.66A1-166[»]
4DSTX-ray2.30A2-167[»]
4DSUX-ray1.70A2-167[»]
4EFLX-ray1.90A1-166[»]
4EFMX-ray1.90A1-166[»]
4EFNX-ray2.30A1-166[»]
4G0NX-ray2.45A1-166[»]
4G3XX-ray3.25A1-166[»]
4K81X-ray2.40B/D/F/H1-166[»]
4L9SX-ray1.61A1-166[»]
4L9WX-ray1.95A1-166[»]
4NYIX-ray2.96Q/R1-166[»]
4NYJX-ray2.85Q/R1-166[»]
4NYMX-ray3.55Q/R1-166[»]
4Q21X-ray2.00A1-189[»]
4RSGneutron diffraction1.91A1-166[»]
4URUX-ray2.83R1-166[»]
4URVX-ray2.58R1-166[»]
4URWX-ray2.76R1-166[»]
4URXX-ray2.49R1-166[»]
4URYX-ray2.47R1-166[»]
4URZX-ray2.24R1-166[»]
4US0X-ray2.17R1-166[»]
4US1X-ray2.65R1-166[»]
4US2X-ray2.48R1-166[»]
4XVQX-ray1.89A1-166[»]
4XVRX-ray2.03A1-166[»]
521PX-ray2.60A1-166[»]
5B2ZX-ray1.56A1-166[»]
5B30X-ray1.60A1-166[»]
5P21X-ray1.35A1-166[»]
621PX-ray2.40A1-166[»]
6Q21X-ray1.95A/B/C/D1-171[»]
721PX-ray2.00A1-166[»]
821PX-ray1.50A1-166[»]
DisProtiDP00153.
ProteinModelPortaliP01112.
SMRiP01112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109501. 91 interactors.
DIPiDIP-1050N.
IntActiP01112. 49 interactors.
MINTiMINT-5002362.
STRINGi9606.ENSP00000309845.

Chemistry databases

BindingDBiP01112.
ChEMBLiCHEMBL2167.
GuidetoPHARMACOLOGYi2822.

PTM databases

iPTMnetiP01112.
PhosphoSitePlusiP01112.
SwissPalmiP01112.

Polymorphism and mutation databases

BioMutaiHRAS.
DMDMi131869.

Proteomic databases

EPDiP01112.
PaxDbiP01112.
PeptideAtlasiP01112.
PRIDEiP01112.

Protocols and materials databases

DNASUi3265.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311189; ENSP00000309845; ENSG00000174775. [P01112-1]
ENST00000397594; ENSP00000380722; ENSG00000174775. [P01112-2]
ENST00000397596; ENSP00000380723; ENSG00000174775. [P01112-1]
ENST00000417302; ENSP00000388246; ENSG00000174775. [P01112-2]
ENST00000451590; ENSP00000407586; ENSG00000174775. [P01112-1]
ENST00000493230; ENSP00000434023; ENSG00000174775. [P01112-2]
ENST00000610977; ENSP00000480686; ENSG00000276536. [P01112-1]
ENST00000615062; ENSP00000482366; ENSG00000276536. [P01112-1]
ENST00000616241; ENSP00000480317; ENSG00000276536. [P01112-2]
ENST00000631404; ENSP00000488757; ENSG00000276536. [P01112-1]
ENST00000631967; ENSP00000488225; ENSG00000276536. [P01112-2]
ENST00000634098; ENSP00000488296; ENSG00000276536. [P01112-2]
GeneIDi3265.
KEGGihsa:3265.
UCSCiuc010qvw.3. human. [P01112-1]

Organism-specific databases

CTDi3265.
DisGeNETi3265.
GeneCardsiHRAS.
GeneReviewsiHRAS.
HGNCiHGNC:5173. HRAS.
HPAiCAB002015.
HPA049830.
MalaCardsiHRAS.
MIMi109800. phenotype.
163200. phenotype.
188470. phenotype.
190020. gene.
218040. phenotype.
neXtProtiNX_P01112.
OpenTargetsiENSG00000174775.
ENSG00000276536.
Orphaneti3071. Costello syndrome.
2612. Linear nevus sebaceus syndrome.
2874. Phakomatosis pigmentokeratotica.
PharmGKBiPA29444.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00860000133672.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP01112.
KOiK02833.
OMAiDCMNCKC.
OrthoDBiEOG091G0UAU.
PhylomeDBiP01112.
TreeFamiTF312796.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000174775-MONOMER.
ReactomeiR-HSA-112412. SOS-mediated signalling.
R-HSA-1169092. Activation of RAS in B cells.
R-HSA-1236382. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
R-HSA-1250196. SHC1 events in ERBB2 signaling.
R-HSA-1250347. SHC1 events in ERBB4 signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-167044. Signalling to RAS.
R-HSA-171007. p38MAPK events.
R-HSA-179812. GRB2 events in EGFR signaling.
R-HSA-180336. SHC1 events in EGFR signaling.
R-HSA-186763. Downstream signal transduction.
R-HSA-1963640. GRB2 events in ERBB2 signaling.
R-HSA-210993. Tie2 Signaling.
R-HSA-2179392. EGFR Transactivation by Gastrin.
R-HSA-2424491. DAP12 signaling.
R-HSA-2428933. SHC-related events triggered by IGF1R.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-5637810. Constitutive Signaling by EGFRvIII.
R-HSA-5654688. SHC-mediated cascade:FGFR1.
R-HSA-5654693. FRS-mediated FGFR1 signaling.
R-HSA-5654699. SHC-mediated cascade:FGFR2.
R-HSA-5654700. FRS-mediated FGFR2 signaling.
R-HSA-5654704. SHC-mediated cascade:FGFR3.
R-HSA-5654706. FRS-mediated FGFR3 signaling.
R-HSA-5654712. FRS-mediated FGFR4 signaling.
R-HSA-5654719. SHC-mediated cascade:FGFR4.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5655291. Signaling by FGFR4 in disease.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5673000. RAF activation.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802953. RAS signaling downstream of NF1 loss-of-function variants.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
R-HSA-74751. Insulin receptor signalling cascade.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
R-HSA-8851805. MET activates RAS signaling.
R-HSA-8853334. Signaling by FGFR3 fusions in cancer.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
SignaLinkiP01112.
SIGNORiP01112.

Miscellaneous databases

EvolutionaryTraceiP01112.
GeneWikiiHRAS.
GenomeRNAii3265.
PROiP01112.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000174775.
CleanExiHS_HRAS.
ExpressionAtlasiP01112. baseline and differential.
GenevisibleiP01112. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRASH_HUMAN
AccessioniPrimary (citable) accession number: P01112
Secondary accession number(s): B5BUA0
, Q14080, Q6FHV9, Q9BR65, Q9UCE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 217 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.