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P01112

- RASH_HUMAN

UniProt

P01112 - RASH_HUMAN

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Protein

GTPase HRas

Gene

HRAS

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTP
Nucleotide bindingi57 – 615GTP
Nucleotide bindingi116 – 1194GTP

GO - Molecular functioni

  1. GTP binding Source: UniProtKB
  2. protein C-terminus binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. activation of MAPKK activity Source: Reactome
  3. axon guidance Source: Reactome
  4. blood coagulation Source: Reactome
  5. cell cycle arrest Source: BHF-UCL
  6. cell proliferation Source: Ensembl
  7. cell surface receptor signaling pathway Source: ProtInc
  8. cellular senescence Source: BHF-UCL
  9. chemotaxis Source: ProtInc
  10. endocytosis Source: Ensembl
  11. epidermal growth factor receptor signaling pathway Source: Reactome
  12. epithelial tube branching involved in lung morphogenesis Source: Ensembl
  13. Fc-epsilon receptor signaling pathway Source: Reactome
  14. fibroblast growth factor receptor signaling pathway Source: Reactome
  15. GTP catabolic process Source: InterPro
  16. innate immune response Source: Reactome
  17. insulin receptor signaling pathway Source: Reactome
  18. intrinsic apoptotic signaling pathway Source: Ensembl
  19. leukocyte migration Source: Reactome
  20. MAPK cascade Source: Reactome
  21. mitotic cell cycle checkpoint Source: BHF-UCL
  22. negative regulation of cell differentiation Source: Ensembl
  23. negative regulation of cell proliferation Source: BHF-UCL
  24. negative regulation of gene expression Source: BHF-UCL
  25. negative regulation of neuron apoptotic process Source: Ensembl
  26. negative regulation of Rho GTPase activity Source: BHF-UCL
  27. neurotrophin TRK receptor signaling pathway Source: Reactome
  28. organ morphogenesis Source: ProtInc
  29. positive regulation of actin cytoskeleton reorganization Source: BHF-UCL
  30. positive regulation of cell migration Source: BHF-UCL
  31. positive regulation of cell proliferation Source: BHF-UCL
  32. positive regulation of DNA replication Source: BHF-UCL
  33. positive regulation of epithelial cell proliferation Source: BHF-UCL
  34. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  35. positive regulation of JNK cascade Source: BHF-UCL
  36. positive regulation of MAPK cascade Source: BHF-UCL
  37. positive regulation of MAP kinase activity Source: BHF-UCL
  38. positive regulation of miRNA metabolic process Source: BHF-UCL
  39. positive regulation of protein phosphorylation Source: BHF-UCL
  40. positive regulation of Rac GTPase activity Source: BHF-UCL
  41. positive regulation of Rac protein signal transduction Source: Ensembl
  42. positive regulation of ruffle assembly Source: BHF-UCL
  43. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  44. positive regulation of wound healing Source: BHF-UCL
  45. protein heterooligomerization Source: Ensembl
  46. Ras protein signal transduction Source: BHF-UCL
  47. regulation of long-term neuronal synaptic plasticity Source: Ensembl
  48. regulation of synaptic transmission, GABAergic Source: Ensembl
  49. signal transduction Source: ProtInc
  50. small GTPase mediated signal transduction Source: Reactome
  51. social behavior Source: Ensembl
  52. striated muscle cell differentiation Source: Ensembl
  53. synaptic transmission Source: Reactome
  54. visual learning Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_115852. Signaling by constitutively active EGFR.
REACT_115854. GRB2 events in ERBB2 signaling.
REACT_115993. SHC1 events in ERBB2 signaling.
REACT_116005. SHC1 events in ERBB4 signaling.
REACT_118778. Activation of RAS in B cells.
REACT_12033. Signalling to RAS.
REACT_12065. p38MAPK events.
REACT_121096. EGFR Transactivation by Gastrin.
REACT_121398. Signaling by FGFR mutants.
REACT_12579. SHC1 events in EGFR signaling.
REACT_12606. GRB2 events in EGFR signaling.
REACT_12621. Tie2 Signaling.
REACT_147814. DAP12 signaling.
REACT_163701. FCERI mediated MAPK activation.
REACT_17025. Downstream signal transduction.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_2077. RAF activation.
REACT_21247. FRS2-mediated cascade.
REACT_21374. SHC-mediated cascade.
REACT_23891. Interleukin receptor SHC signaling.
REACT_524. SOS-mediated signalling.
REACT_614. RAF phosphorylates MEK.
REACT_661. SHC-mediated signalling.
REACT_962. MEK activation.
SignaLinkiP01112.

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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:5173. HRAS.

Subcellular locationi

Cell membrane. Cell membrane; 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.By similarity
Isoform 2 : Nucleus. Cytoplasm. Cytoplasmperinuclear region
Note: Colocalizes with GNB2L1 to the perinuclear region.

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. Golgi apparatus Source: UniProtKB
  4. nucleus Source: UniProtKB-KW
  5. 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) [MIM:218040]: 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.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121G → A in CSTLO. 3 Publications
VAR_026106
Natural varianti12 – 121G → C in CSTLO. 2 Publications
VAR_045975
Natural varianti12 – 121G → D in CSTLO; severe mutation. 1 Publication
VAR_068816
Natural varianti12 – 121G → E in CSTLO. 1 Publication
VAR_045976
Natural varianti12 – 121G → S in CSTLO, OSCC and CMEMS. 6 Publications
VAR_006837
Natural varianti12 – 121G → 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. 2 Publications
VAR_006836
Natural varianti13 – 131G → C in CSTLO. 1 Publication
VAR_026107
Natural varianti13 – 131G → D in CSTLO. 1 Publication
VAR_026108
Natural varianti58 – 581T → I in CSTLO. 1 Publication
VAR_045978
Natural varianti117 – 1171K → R in CSTLO. 1 Publication
VAR_045981
Natural varianti146 – 1461A → T in CSTLO. 1 Publication
VAR_045982
Natural varianti146 – 1461A → V in CSTLO. 1 Publication
VAR_045983
Congenital myopathy with excess of muscle spindles (CMEMS) [MIM:218040]: Variant of Costello syndrome.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121G → S in CSTLO, OSCC and CMEMS. 6 Publications
VAR_006837
Natural varianti12 – 121G → 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. 2 Publications
VAR_006836
Natural varianti22 – 221Q → K in CMEMS. 1 Publication
VAR_045977
Natural varianti63 – 631E → K in CMEMS. 1 Publication
VAR_045980
Hurthle cell thyroid carcinoma (HCTC) [MIM:607464]: A rare type of thyroid cancer accounting for only about 3-10% of all differentiated thyroid cancers. These neoplasms are considered a variant of follicular carcinoma of the thyroid and are referred to as follicular carcinoma, oxyphilic type.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
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) [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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Defects in HRAS are the cause of oral squamous cell carcinoma (OSCC).
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. 1 Publication
VAR_068817

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171S → N: Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2. 2 Publications
Mutagenesisi26 – 261N → G: Loss of interaction with PLCE1; when associated with V-12. 1 Publication
Mutagenesisi29 – 291V → A: No effect on interaction with PLCE1; when associated with V-12. 1 Publication
Mutagenesisi32 – 321Y → F: Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12. 1 Publication
Mutagenesisi34 – 341P → G: No effect on interaction with PLCE1; when associated with V-12. 1 Publication
Mutagenesisi35 – 351T → S: Loss of interaction with PLCE1; when associated with V-12. 1 Publication
Mutagenesisi37 – 371E → G: No effect on interaction with PLCE1; when associated with V-12. 1 Publication
Mutagenesisi38 – 381D → N: No effect on interaction with PLCE1; when associated with V-12. 1 Publication
Mutagenesisi39 – 391S → C: No effect on interaction with PLCE1; when associated with V-12. 1 Publication
Mutagenesisi59 – 591A → T: Loss of GTPase activity and creation of an autophosphorylation site.
Mutagenesisi61 – 611Q → I: Moderately increased transformation of cultured cell lines. 1 Publication
Mutagenesisi61 – 611Q → V: Strongly increased transformation of cultured cell lines. 1 Publication
Mutagenesisi83 – 831A → T: GTP-binding activity reduced by factor of 30. 1 Publication
Mutagenesisi118 – 1181C → S: Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange. 2 Publications
Mutagenesisi119 – 1191D → N: Loss of GTP-binding activity. 1 Publication
Mutagenesisi144 – 1441T → I: GTP-binding activity reduced by factor of 25. 1 Publication
Mutagenesisi164 – 1652RQ → AV: Loss of GTP-binding activity. 1 Publication
Mutagenesisi181 – 1811C → S: Exclusively localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-184. 2 Publications
Mutagenesisi184 – 1841C → 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 Publications

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

MIMi109800. phenotype.
163200. phenotype.
218040. phenotype.
607464. phenotype.
Orphaneti3071. Costello syndrome.
2612. Linear nevus sebaceus syndrome.
2874. Phakomatosis pigmentokeratotica.
PharmGKBiPA29444.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 186186GTPase HRasPRO_0000042996Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 186185GTPase HRas, N-terminally processedPRO_0000326476Add
BLAST
Propeptidei187 – 1893Removed in mature formPRO_0000042997

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in GTPase HRas; alternate1 Publication
Modified residuei2 – 21N-acetylthreonine; in GTPase HRas, N-terminally processed1 Publication
Modified residuei118 – 1181S-nitrosocysteine1 Publication
Lipidationi181 – 1811S-palmitoyl cysteine4 Publications
Lipidationi184 – 1841S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate1 Publication
Lipidationi184 – 1841S-palmitoyl cysteine; alternate4 Publications
Modified residuei186 – 1861Cysteine methyl ester1 Publication
Lipidationi186 – 1861S-farnesyl cysteine1 Publication

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

MaxQBiP01112.
PaxDbiP01112.
PRIDEiP01112.

PTM databases

PhosphoSiteiP01112.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiP01112.
CleanExiHS_HRAS.
ExpressionAtlasiP01112. baseline and differential.
GenevestigatoriP01112.

Organism-specific databases

HPAiCAB002015.

Interactioni

Subunit structurei

In its GTP-bound form interacts with PLCE1. Interacts with TBC1D10C. Interacts with RGL3. Interacts with HSPD1. Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) By similarity. Forms a signaling complex with RASGRP1 and DGKZ. Interacts with RASSF5. Interacts with PDE6D. Interacts with IKZF3. Interacts with GNB2L1. 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.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

Protein-protein interaction databases

BioGridi109501. 68 interactions.
DIPiDIP-1050N.
IntActiP01112. 28 interactions.
MINTiMINT-5002362.
STRINGi9606.ENSP00000309845.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119
Beta strandi12 – 143
Helixi16 – 2510
Beta strandi27 – 315
Beta strandi34 – 374
Beta strandi38 – 469
Beta strandi49 – 579
Beta strandi60 – 634
Helixi66 – 749
Beta strandi76 – 838
Turni84 – 863
Helixi87 – 10418
Beta strandi105 – 1073
Beta strandi111 – 1166
Beta strandi120 – 1223
Helixi127 – 13610
Beta strandi141 – 1444
Turni146 – 1483
Helixi152 – 16413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
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[»]
521PX-ray2.60A1-166[»]
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. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01112.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 18520Hypervariable regionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118909.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP01112.
KOiK02833.
OMAiYPCIRRP.
OrthoDBiEOG7QVM41.
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]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. 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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121G → A in CSTLO. 3 Publications
VAR_026106
Natural varianti12 – 121G → C in CSTLO. 2 Publications
VAR_045975
Natural varianti12 – 121G → D in CSTLO; severe mutation. 1 Publication
VAR_068816
Natural varianti12 – 121G → E in CSTLO. 1 Publication
VAR_045976
Natural varianti12 – 121G → S in CSTLO, OSCC and CMEMS. 6 Publications
VAR_006837
Natural varianti12 – 121G → 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. 2 Publications
VAR_006836
Natural varianti13 – 131G → C in CSTLO. 1 Publication
VAR_026107
Natural varianti13 – 131G → D in CSTLO. 1 Publication
VAR_026108
Natural varianti13 – 131G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. 1 Publication
VAR_068817
Natural varianti22 – 221Q → K in CMEMS. 1 Publication
VAR_045977
Natural varianti37 – 371E → EE in FCSS. 1 Publication
VAR_068818
Natural varianti58 – 581T → I in CSTLO. 1 Publication
VAR_045978
Natural varianti61 – 611Q → K in follicular thyroid carcinoma samples; somatic mutation; increases transformation of cultured cell lines. 1 Publication
Corresponds to variant rs28933406 [ dbSNP | Ensembl ].
VAR_045979
Natural varianti61 – 611Q → L in melanoma; strongly reduced GTP hydrolysis in the presence of RAF1; increases transformation of cultured cell lines.
VAR_006838
Natural varianti63 – 631E → K in CMEMS. 1 Publication
VAR_045980
Natural varianti117 – 1171K → R in CSTLO. 1 Publication
VAR_045981
Natural varianti146 – 1461A → T in CSTLO. 1 Publication
VAR_045982
Natural varianti146 – 1461A → V in CSTLO. 1 Publication
VAR_045983

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 18938VEDAF…KCVLS → SRSGSSSSSGTLWDPPGPM in isoform 2. 2 PublicationsVSP_041597Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_001130442.1. [P01112-1]
NP_005334.1. NM_005343.2. [P01112-1]
NP_789765.1. NM_176795.3. [P01112-2]
XP_006718280.1. XM_006718217.1. [P01112-2]
XP_006725199.1. XM_006725136.1. [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]
GeneIDi3265.
KEGGihsa:3265.
UCSCiuc001lpv.3. human. [P01112-1]
uc010qvw.2. human. [P01112-2]

Polymorphism databases

DMDMi131869.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7698.1. [P01112-1 ]
CCDS7699.1. [P01112-2 ]
PIRi A93299. TVHUH.
RefSeqi NP_001123914.1. NM_001130442.1. [P01112-1 ]
NP_005334.1. NM_005343.2. [P01112-1 ]
NP_789765.1. NM_176795.3. [P01112-2 ]
XP_006718280.1. XM_006718217.1. [P01112-2 ]
XP_006725199.1. XM_006725136.1. [P01112-2 ]
UniGenei Hs.37003.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
121P X-ray 1.54 A 1-166 [» ]
1AA9 NMR - A 1-171 [» ]
1AGP X-ray 2.30 A 1-166 [» ]
1BKD X-ray 2.80 R 1-166 [» ]
1CLU X-ray 1.70 A 1-166 [» ]
1CRP NMR - A 1-166 [» ]
1CRQ NMR - A 1-166 [» ]
1CRR NMR - A 1-166 [» ]
1CTQ X-ray 1.26 A 1-166 [» ]
1GNP X-ray 2.70 A 1-166 [» ]
1GNQ X-ray 2.50 A 1-166 [» ]
1GNR X-ray 1.85 A 1-166 [» ]
1HE8 X-ray 3.00 B 1-166 [» ]
1IAQ X-ray 2.90 A/B/C 1-166 [» ]
1IOZ X-ray 2.00 A 1-171 [» ]
1JAH X-ray 1.80 A 1-166 [» ]
1JAI X-ray 1.80 A 1-166 [» ]
1K8R X-ray 3.00 A 1-166 [» ]
1LF0 X-ray 1.70 A 1-166 [» ]
1LF5 X-ray 1.70 A 1-166 [» ]
1LFD X-ray 2.10 B/D 1-167 [» ]
1NVU X-ray 2.20 Q/R 1-166 [» ]
1NVV X-ray 2.18 Q/R 1-166 [» ]
1NVW X-ray 2.70 Q/R 1-166 [» ]
1NVX X-ray 3.20 Q/R 1-166 [» ]
1P2S X-ray 2.45 A 1-166 [» ]
1P2T X-ray 2.00 A 1-166 [» ]
1P2U X-ray 2.00 A 1-166 [» ]
1P2V X-ray 2.30 A 1-166 [» ]
1PLJ X-ray 2.80 A 1-166 [» ]
1PLK X-ray 2.80 A 1-166 [» ]
1PLL X-ray 2.80 A 1-166 [» ]
1Q21 X-ray 2.20 A 1-171 [» ]
1QRA X-ray 1.60 A 1-166 [» ]
1RVD X-ray 1.90 A 1-166 [» ]
1WQ1 X-ray 2.50 R 1-166 [» ]
1XCM X-ray 1.84 A 1-167 [» ]
1XD2 X-ray 2.70 A/B 1-166 [» ]
1XJ0 X-ray 1.70 A 1-166 [» ]
1ZVQ X-ray 2.00 A 1-166 [» ]
1ZW6 X-ray 1.50 A 1-166 [» ]
221P X-ray 2.30 A 1-166 [» ]
2C5L X-ray 1.90 A/B 1-166 [» ]
2CE2 X-ray 1.00 X 1-166 [» ]
2CL0 X-ray 1.80 X 1-166 [» ]
2CL6 X-ray 1.24 X 1-166 [» ]
2CL7 X-ray 1.25 X 1-166 [» ]
2CLC X-ray 1.30 X 1-166 [» ]
2CLD X-ray 1.22 X 1-166 [» ]
2EVW X-ray 1.05 X 1-166 [» ]
2GDP model - A 1-171 [» ]
2LCF NMR - A 1-166 [» ]
2LWI NMR - A 1-166 [» ]
2Q21 X-ray 2.20 A 1-171 [» ]
2QUZ X-ray 1.49 A 1-166 [» ]
2RGA X-ray 1.90 A 1-166 [» ]
2RGB X-ray 1.35 A 1-166 [» ]
2RGC X-ray 1.60 A 1-166 [» ]
2RGD X-ray 2.00 A 1-166 [» ]
2RGE X-ray 1.40 A 1-166 [» ]
2RGG X-ray 1.45 A 1-166 [» ]
2UZI X-ray 2.00 R 1-166 [» ]
2VH5 X-ray 2.70 R 1-166 [» ]
2X1V X-ray 1.70 A 1-166 [» ]
3DDC X-ray 1.80 A 1-166 [» ]
3I3S X-ray 1.36 R 1-166 [» ]
3K8Y X-ray 1.30 A 1-166 [» ]
3K9L X-ray 1.80 A/B/C 1-166 [» ]
3K9N X-ray 2.00 A 1-166 [» ]
3KKM X-ray 1.70 A 1-166 [» ]
3KKN X-ray 2.09 A 1-166 [» ]
3KUD X-ray 2.15 A 1-166 [» ]
3L8Y X-ray 2.02 A 1-166 [» ]
3L8Z X-ray 1.44 A 1-166 [» ]
3LBH X-ray 1.85 A 1-166 [» ]
3LBI X-ray 2.09 A 1-166 [» ]
3LBN X-ray 1.86 A 1-166 [» ]
3LO5 X-ray 2.57 A/C/E 1-166 [» ]
3OIU X-ray 1.32 A 1-166 [» ]
3OIV X-ray 1.84 A 1-166 [» ]
3OIW X-ray 1.30 A 1-166 [» ]
3RRY X-ray 1.60 A 1-166 [» ]
3RRZ X-ray 1.60 A 1-166 [» ]
3RS0 X-ray 1.40 A 1-166 [» ]
3RS2 X-ray 1.84 A 1-166 [» ]
3RS3 X-ray 1.52 A 1-166 [» ]
3RS4 X-ray 1.70 A 1-166 [» ]
3RS5 X-ray 1.68 A 1-166 [» ]
3RS7 X-ray 1.70 A 1-166 [» ]
3RSL X-ray 1.70 A 1-166 [» ]
3RSO X-ray 1.60 A 1-166 [» ]
3TGP X-ray 1.31 A 1-166 [» ]
421P X-ray 2.20 A 1-166 [» ]
4DLR X-ray 1.32 A 1-166 [» ]
4DLS X-ray 1.82 A 1-166 [» ]
4DLT X-ray 1.70 A 1-166 [» ]
4DLU X-ray 1.60 A 1-166 [» ]
4DLV X-ray 1.57 A 1-166 [» ]
4DLW X-ray 1.72 A 1-166 [» ]
4DLX X-ray 1.73 A 1-166 [» ]
4DLY X-ray 1.57 A 1-166 [» ]
4DLZ X-ray 1.66 A 1-166 [» ]
4DST X-ray 2.30 A 2-167 [» ]
4DSU X-ray 1.70 A 2-167 [» ]
4EFL X-ray 1.90 A 1-166 [» ]
4EFM X-ray 1.90 A 1-166 [» ]
4EFN X-ray 2.30 A 1-166 [» ]
4G0N X-ray 2.45 A 1-166 [» ]
4G3X X-ray 3.25 A 1-166 [» ]
4K81 X-ray 2.40 B/D/F/H 1-166 [» ]
4L9S X-ray 1.61 A 1-166 [» ]
4L9W X-ray 1.95 A 1-166 [» ]
4NYI X-ray 2.96 Q/R 1-166 [» ]
4NYJ X-ray 2.85 Q/R 1-166 [» ]
4NYM X-ray 3.55 Q/R 1-166 [» ]
4Q21 X-ray 2.00 A 1-189 [» ]
521P X-ray 2.60 A 1-166 [» ]
5P21 X-ray 1.35 A 1-166 [» ]
621P X-ray 2.40 A 1-166 [» ]
6Q21 X-ray 1.95 A/B/C/D 1-171 [» ]
721P X-ray 2.00 A 1-166 [» ]
821P X-ray 1.50 A 1-166 [» ]
DisProti DP00153.
ProteinModelPortali P01112.
SMRi P01112. Positions 1-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109501. 68 interactions.
DIPi DIP-1050N.
IntActi P01112. 28 interactions.
MINTi MINT-5002362.
STRINGi 9606.ENSP00000309845.

Chemistry

BindingDBi P01112.
ChEMBLi CHEMBL2167.

PTM databases

PhosphoSitei P01112.

Polymorphism databases

DMDMi 131869.

Proteomic databases

MaxQBi P01112.
PaxDbi P01112.
PRIDEi P01112.

Protocols and materials databases

DNASUi 3265.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311189 ; 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 ]
GeneIDi 3265.
KEGGi hsa:3265.
UCSCi uc001lpv.3. human. [P01112-1 ]
uc010qvw.2. human. [P01112-2 ]

Organism-specific databases

CTDi 3265.
GeneCardsi GC11M000522.
GeneReviewsi HRAS.
HGNCi HGNC:5173. HRAS.
HPAi CAB002015.
MIMi 109800. phenotype.
163200. phenotype.
190020. gene.
218040. phenotype.
607464. phenotype.
neXtProti NX_P01112.
Orphaneti 3071. Costello syndrome.
2612. Linear nevus sebaceus syndrome.
2874. Phakomatosis pigmentokeratotica.
PharmGKBi PA29444.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000118909.
HOGENOMi HOG000233973.
HOVERGENi HBG009351.
InParanoidi P01112.
KOi K02833.
OMAi YPCIRRP.
OrthoDBi EOG7QVM41.
PhylomeDBi P01112.
TreeFami TF312796.

Enzyme and pathway databases

Reactomei REACT_111040. Signaling by SCF-KIT.
REACT_115852. Signaling by constitutively active EGFR.
REACT_115854. GRB2 events in ERBB2 signaling.
REACT_115993. SHC1 events in ERBB2 signaling.
REACT_116005. SHC1 events in ERBB4 signaling.
REACT_118778. Activation of RAS in B cells.
REACT_12033. Signalling to RAS.
REACT_12065. p38MAPK events.
REACT_121096. EGFR Transactivation by Gastrin.
REACT_121398. Signaling by FGFR mutants.
REACT_12579. SHC1 events in EGFR signaling.
REACT_12606. GRB2 events in EGFR signaling.
REACT_12621. Tie2 Signaling.
REACT_147814. DAP12 signaling.
REACT_163701. FCERI mediated MAPK activation.
REACT_17025. Downstream signal transduction.
REACT_18334. NCAM signaling for neurite out-growth.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_2077. RAF activation.
REACT_21247. FRS2-mediated cascade.
REACT_21374. SHC-mediated cascade.
REACT_23891. Interleukin receptor SHC signaling.
REACT_524. SOS-mediated signalling.
REACT_614. RAF phosphorylates MEK.
REACT_661. SHC-mediated signalling.
REACT_962. MEK activation.
SignaLinki P01112.

Miscellaneous databases

EvolutionaryTracei P01112.
GeneWikii HRAS.
GenomeRNAii 3265.
NextBioi 12961.
PROi P01112.
SOURCEi Search...

Gene expression databases

Bgeei P01112.
CleanExi HS_HRAS.
ExpressionAtlasi P01112. baseline and differential.
Genevestigatori P01112.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view ]
PANTHERi PTHR24070. PTHR24070. 1 hit.
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00173. RAS. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51421. RAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue."
    Capon D.J., Chen E.Y., Levinson A.D., Seeburg P.H., Goeddel D.V.
    Nature 302:33-37(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence analysis of the T24 human bladder carcinoma oncogene."
    Reddy E.P.
    Science 220:1061-1063(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Molecular cloning and the total nucleotide sequence of the human c-Ha-ras-1 gene activated in a melanoma from a Japanese patient."
    Sekiya T., Fushimi M., Hori H., Hirohashi S., Nishimura S., Sugimura T.
    Proc. Natl. Acad. Sci. U.S.A. 81:4771-4775(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus."
    Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D., Ferrer J.C., Guinovart J.J., Bach-Elias M.
    Cancer Res. 63:5178-5187(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH GNB2L1, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, MUTAGENESIS OF SER-17.
  5. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. NIEHS SNPs program
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lung carcinoma.
  12. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-41; 43-117; 129-161 AND 170-185, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  13. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
  14. "Identification of the principal promoter sequence of the c-H-ras transforming oncogene: deletion analysis of the 5'-flanking region by focus formation assay."
    Honkawa H., Masahashi W., Hashimoto S., Hashimoto-Gotoh T.
    Mol. Cell. Biol. 7:2933-2940(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
  15. "Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP."
    Loew A., Sprinzl M., Faulhammer H.G.
    Eur. J. Biochem. 215:473-479(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 108-117 AND 132-153.
  16. "Isolation of ras GTP-binding mutants using an in situ colony-binding assay."
    Feig L.A., Pan B.-T., Roberts T.M., Cooper G.M.
    Proc. Natl. Acad. Sci. U.S.A. 83:4607-4611(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ALA-83; ASP-119 AND THR-144.
  17. "Deletion mutants of Harvey ras p21 protein reveal the absolute requirement of at least two distant regions for GTP-binding and transforming activities."
    Lacal J.C., Anderson P.S., Aaronson S.A.
    EMBO J. 5:679-687(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 164-ARG-GLN-165.
  18. "All ras proteins are polyisoprenylated but only some are palmitoylated."
    Hancock J.F., Magee A.I., Childs J.E., Marshall C.J.
    Cell 57:1167-1177(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-181 AND CYS-184.
  19. "Palmitoylation of Ha-Ras facilitates membrane binding, activation of downstream effectors, and meiotic maturation in Xenopus oocytes."
    Dudler T., Gelb M.H.
    J. Biol. Chem. 271:11541-11547(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-181 AND CYS-184, ISOPRENYLATION AT CYS-186, METHYLATION AT CYS-186, MUTAGENESIS OF CYS-181 AND CYS-184.
  20. "A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction."
    Lander H.M., Hajjar D.P., Hempstead B.L., Mirza U.A., Chait B.T., Campbell S., Quilliam L.A.
    J. Biol. Chem. 272:4323-4326(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-118, FUNCTION, MASS SPECTROMETRY, MUTAGENESIS OF CYS-118.
  21. "Aiolos transcription factor controls cell death in T cells by regulating Bcl-2 expression and its cellular localization."
    Romero F., Martinez-A C., Camonis J., Rebollo A.
    EMBO J. 18:3419-3430(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKZF3.
  22. "RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a Ras/Rap1A-associating domain, is conserved between nematode and humans."
    Liao Y., Kariya K., Hu C.-D., Shibatohge M., Goshima M., Okada T., Watari Y., Gao X., Jin T.-G., Yamawaki-Kataoka Y., Kataoka T.
    J. Biol. Chem. 274:37815-37820(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAPGEF2.
  23. "Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras."
    Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y., Shibatohge M., Wu D., Satoh T., Kataoka T.
    J. Biol. Chem. 276:2752-2757(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLCE1, CHARACTERIZATION OF VARIANT VAL-12, MUTAGENESIS OF SER-17; ASN-26; VAL-29; TYR-32; PRO-34; THR-35; GLU-37; ASP-38 AND SER-39.
  24. "Nedd4 regulates ubiquitination and stability of the guanine-nucleotide exchange factor CNrasGEF."
    Pham N., Rotin D.
    J. Biol. Chem. 276:46995-47003(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAPGEF2.
  25. "Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism."
    Topham M.K., Prescott S.M.
    J. Cell Biol. 152:1135-1143(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH RASGRP1 AND DGKZ.
  26. "The complex of Arl2-GTP and PDE delta: from structure to function."
    Hanzal-Bayer M., Renault L., Roversi P., Wittinghofer A., Hillig R.C.
    EMBO J. 21:2095-2106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDE6D.
  27. "The cyclopentenone 15-deoxy-delta 12,14-prostaglandin J2 binds to and activates H-Ras."
    Oliva J.L., Perez-Sala D., Castrillo A., Martinez N., Canada F.J., Bosca L., Rojas J.M.
    Proc. Natl. Acad. Sci. U.S.A. 100:4772-4777(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPIDATION AT CYS-184, MUTAGENESIS OF CYS-184.
  28. "Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease."
    Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.
    J. Biol. Chem. 280:1790-1796(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF CSTLO VARIANT VAL-12.
  29. "DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras."
    Swarthout J.T., Lobo S., Farh L., Croke M.R., Greentree W.K., Deschenes R.J., Linder M.E.
    J. Biol. Chem. 280:31141-31148(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-181 AND CYS-184.
  30. "An acylation cycle regulates localization and activity of palmitoylated Ras isoforms."
    Rocks O., Peyker A., Kahms M., Verveer P.J., Koerner C., Lumbierres M., Kuhlmann J., Waldmann H., Wittinghofer A., Bastiaens P.I.H.
    Science 307:1746-1752(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-181 AND CYS-184, MUTAGENESIS OF CYS-181 AND CYS-184, SUBCELLULAR LOCATION.
  31. "Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin."
    Pan F., Sun L., Kardian D.B., Whartenby K.A., Pardoll D.M., Liu J.O.
    Nature 445:433-436(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TBC1D10C.
  32. "Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21."
    de Vos A.M., Tong L., Milburn M.V., Matias P.M., Jancarik J., Noguchi S., Nishimura S., Miura K., Ohtsuka E., Kim S.-H.
    Science 239:888-893(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  33. "Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation."
    Pai E.F., Kabsch W., Krengel U., Holmes K.C., John J., Wittinghofer A.
    Nature 341:209-214(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  34. "Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35-A resolution: implications for the mechanism of GTP hydrolysis."
    Pai E.F., Krengel U., Petsko G.A., Goody R.S., Kabsch W., Wittinghofer A.
    EMBO J. 9:2351-2359(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
  35. "Crystal structures at 2.2-A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP."
    Tong L.A., de Vos A.M., Milburn M.V., Kim S.H.
    J. Mol. Biol. 217:503-516(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  36. "Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy."
    Kraulis P.J., Domaille P.J., Campbell-Burk S.L., van Aken T., Laue E.D.
    Biochemistry 33:3515-3531(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-166.
  37. "The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants."
    Scheffzek K., Ahmadian M.R., Kabsch W., Wiesmuller L., Lautwein A., Schmitz F., Wittinghofer A.
    Science 277:333-338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-166 IN COMPLEX WITH RASGAP.
  38. "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."
    Scheidig A.J., Burmester C., Goody R.S.
    Structure 7:1311-1324(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS).
  39. "The structural basis for the transition from Ras-GTP to Ras-GDP."
    Hall B.E., Bar-Sagi D., Nassar N.
    Proc. Natl. Acad. Sci. U.S.A. 99:12138-12142(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-166 IN COMPLEXES WITH GTP ANALOGS.
  40. "Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange."
    Williams J.G., Pappu K., Campbell S.L.
    Proc. Natl. Acad. Sci. U.S.A. 100:6376-6381(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-166, S-NITROSYLATION, FUNCTION, MUTAGENESIS OF CYS-118, IDENTIFICATION BY MASS SPECTROMETRY.
  41. "Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf."
    Buhrman G., Wink G., Mattos C.
    Structure 15:1618-1629(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-166 IN COMPLEXES WITH GTP ANALOG, CHARACTERIZATION OF VARIANTS LEU-61 AND LYS-61, MUTAGENESIS OF GLN-61.
  42. "Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II."
    Stieglitz B., Bee C., Schwarz D., Yildiz O., Moshnikova A., Khokhlatchev A., Herrmann C.
    EMBO J. 27:1995-2005(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-166 IN COMPLEX WITH RASSF5.
  43. "The p53 tumor-suppressor gene and ras oncogene mutations in oral squamous-cell carcinoma."
    Sakai E., Rikimaru K., Ueda M., Matsumoto Y., Ishii N., Enomoto S., Yamamoto H., Tsuchida N.
    Int. J. Cancer 52:867-872(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OSCC SER-12.
  44. "RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma."
    Nikiforova M.N., Lynch R.A., Biddinger P.W., Alexander E.K., Dorn G.W. II, Tallini G., Kroll T.G., Nikiforov Y.E.
    J. Clin. Endocrinol. Metab. 88:2318-2326(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LYS-61, INVOLVEMENT IN SUSCEPTIBILITY TO HURTHLE CELL THYROID CARCINOMA.
  45. Cited for: VARIANTS CSTLO ALA-12; SER-12; VAL-12 AND ASP-13.
  46. Cited for: VARIANTS CSTLO ALA-12; SER-12 AND CYS-13.
  47. Cited for: VARIANTS CSTLO SER-12; CYS-12; GLU-12; ALA-12 AND ARG-117.
  48. Cited for: VARIANTS CSTLO SER-12 AND THR-146.
  49. "Myopathy caused by HRAS germline mutations: implications for disturbed myogenic differentiation in the presence of constitutive HRas activation."
    van der Burgt I., Kupsky W., Stassou S., Nadroo A., Barroso C., Diem A., Kratz C.P., Dvorsky R., Ahmadian M.R., Zenker M.
    J. Med. Genet. 44:459-462(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CMEMS VAL-12; SER-12; LYS-22 AND LYS-63.
  50. Cited for: VARIANTS CSTLO ILE-58 AND VAL-146.
  51. Cited for: VARIANTS CSTLO ASP-12 AND CYS-12.
  52. "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."
    Gremer L., De Luca A., Merbitz-Zahradnik T., Dallapiccola B., Morlot S., Tartaglia M., Kutsche K., Ahmadian M.R., Rosenberger G.
    Hum. Mol. Genet. 19:790-802(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSTLO GLU-37 INS.
  53. Cited for: VARIANT SFM ARG-13, CHARACTERIZATION OF VARIANT SFM ARG-13.

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: October 29, 2014
This is version 193 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

External Data

Dasty 3