SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P01112

- RASH_HUMAN

UniProt

P01112 - RASH_HUMAN

Protein

GTPase HRas

Gene

HRAS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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 binding Source: UniProtKB
    3. 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. Fc-epsilon receptor signaling pathway Source: Reactome
    13. fibroblast growth factor receptor signaling pathway Source: Reactome
    14. GTP catabolic process Source: InterPro
    15. innate immune response Source: Reactome
    16. insulin receptor signaling pathway Source: Reactome
    17. intrinsic apoptotic signaling pathway Source: Ensembl
    18. leukocyte migration Source: Reactome
    19. MAPK cascade Source: Reactome
    20. mitotic cell cycle checkpoint Source: BHF-UCL
    21. negative regulation of cell proliferation Source: BHF-UCL
    22. negative regulation of gene expression Source: BHF-UCL
    23. negative regulation of neuron apoptotic process Source: Ensembl
    24. negative regulation of Rho GTPase activity Source: BHF-UCL
    25. neurotrophin TRK receptor signaling pathway Source: Reactome
    26. organ morphogenesis Source: ProtInc
    27. positive regulation of actin cytoskeleton reorganization Source: BHF-UCL
    28. positive regulation of cell migration Source: BHF-UCL
    29. positive regulation of cell proliferation Source: BHF-UCL
    30. positive regulation of DNA replication Source: BHF-UCL
    31. positive regulation of epithelial cell proliferation Source: BHF-UCL
    32. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    33. positive regulation of JNK cascade Source: BHF-UCL
    34. positive regulation of MAPK cascade Source: BHF-UCL
    35. positive regulation of MAP kinase activity Source: BHF-UCL
    36. positive regulation of miRNA metabolic process Source: BHF-UCL
    37. positive regulation of protein phosphorylation Source: BHF-UCL
    38. positive regulation of Rac GTPase activity Source: BHF-UCL
    39. positive regulation of Rac protein signal transduction Source: Ensembl
    40. positive regulation of ruffle assembly Source: BHF-UCL
    41. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    42. positive regulation of wound healing Source: BHF-UCL
    43. protein heterooligomerization Source: Ensembl
    44. Ras protein signal transduction Source: BHF-UCL
    45. regulation of long-term neuronal synaptic plasticity Source: Ensembl
    46. regulation of synaptic transmission, GABAergic Source: Ensembl
    47. signal transduction Source: ProtInc
    48. small GTPase mediated signal transduction Source: Reactome
    49. social behavior Source: Ensembl
    50. striated muscle cell differentiation Source: Ensembl
    51. synaptic transmission Source: Reactome
    52. visual learning Source: Ensembl

    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

    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. Golgi membrane Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB-SubCell
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Faciocutaneoskeletal syndrome (FCSS) [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 FCSS. 3 Publications
    VAR_026106
    Natural varianti12 – 121G → C in FCSS. 2 Publications
    VAR_045975
    Natural varianti12 – 121G → D in FCSS; severe mutation. 1 Publication
    VAR_068816
    Natural varianti12 – 121G → E in FCSS. 1 Publication
    VAR_045976
    Natural varianti12 – 121G → S in FCSS, OSCC and CMEMS. 6 Publications
    VAR_006837
    Natural varianti12 – 121G → V in FCSS, 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 FCSS. 1 Publication
    VAR_026107
    Natural varianti13 – 131G → D in FCSS. 1 Publication
    VAR_026108
    Natural varianti37 – 371E → EE in FCSS. 1 Publication
    VAR_068818
    Natural varianti58 – 581T → I in FCSS. 1 Publication
    VAR_045978
    Natural varianti117 – 1171K → R in FCSS. 1 Publication
    VAR_045981
    Natural varianti146 – 1461A → T in FCSS. 1 Publication
    VAR_045982
    Natural varianti146 – 1461A → V in FCSS. 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 FCSS, OSCC and CMEMS. 6 Publications
    VAR_006837
    Natural varianti12 – 121G → V in FCSS, 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. 3 Publications
    Mutagenesisi26 – 261N → G: Loss of interaction with PLCE1; when associated with V-12. 2 Publications
    Mutagenesisi29 – 291V → A: No effect on interaction with PLCE1; when associated with V-12. 2 Publications
    Mutagenesisi32 – 321Y → F: Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12. 2 Publications
    Mutagenesisi34 – 341P → G: No effect on interaction with PLCE1; when associated with V-12. 2 Publications
    Mutagenesisi35 – 351T → S: Loss of interaction with PLCE1; when associated with V-12. 2 Publications
    Mutagenesisi37 – 371E → G: No effect on interaction with PLCE1; when associated with V-12. 2 Publications
    Mutagenesisi38 – 381D → N: No effect on interaction with PLCE1; when associated with V-12. 2 Publications
    Mutagenesisi39 – 391S → C: No effect on interaction with PLCE1; when associated with V-12. 2 Publications
    Mutagenesisi59 – 591A → T: Loss of GTPase activity and creation of an autophosphorylation site. 1 Publication
    Mutagenesisi61 – 611Q → I: Moderately increased transformation of cultured cell lines. 2 Publications
    Mutagenesisi61 – 611Q → V: Strongly increased transformation of cultured cell lines. 2 Publications
    Mutagenesisi83 – 831A → T: GTP-binding activity reduced by factor of 30. 2 Publications
    Mutagenesisi118 – 1181C → S: Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange. 3 Publications
    Mutagenesisi119 – 1191D → N: Loss of GTP-binding activity. 2 Publications
    Mutagenesisi144 – 1441T → I: GTP-binding activity reduced by factor of 25. 2 Publications
    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. 3 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. 4 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-nitrosocysteine2 Publications
    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

    ArrayExpressiP01112.
    BgeeiP01112.
    CleanExiHS_HRAS.
    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. 58 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.
    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]
    ProtoNetiSearch...

    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

    MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET    50
    CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI 100
    KRVKDSDDVP MVLVGNKCDL AARTVESRQA QDLARSYGIP YIETSAKTRQ 150
    GVEDAFYTLV REIRQHKLRK LNPPDESGPG CMSCKCVLS 189
    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 FCSS. 3 Publications
    VAR_026106
    Natural varianti12 – 121G → C in FCSS. 2 Publications
    VAR_045975
    Natural varianti12 – 121G → D in FCSS; severe mutation. 1 Publication
    VAR_068816
    Natural varianti12 – 121G → E in FCSS. 1 Publication
    VAR_045976
    Natural varianti12 – 121G → S in FCSS, OSCC and CMEMS. 6 Publications
    VAR_006837
    Natural varianti12 – 121G → V in FCSS, 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 FCSS. 1 Publication
    VAR_026107
    Natural varianti13 – 131G → D in FCSS. 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 FCSS. 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 FCSS. 1 Publication
    VAR_045981
    Natural varianti146 – 1461A → T in FCSS. 1 Publication
    VAR_045982
    Natural varianti146 – 1461A → V in FCSS. 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. 58 interactions.
    DIPi DIP-1050N.
    IntActi P01112. 28 interactions.
    MINTi MINT-5002362.
    STRINGi 9606.ENSP00000309845.

    Chemistry

    BindingDBi P01112.
    ChEMBLi CHEMBL2167.
    DrugBanki DB00605. Sulindac.

    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.
    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

    ArrayExpressi P01112.
    Bgeei P01112.
    CleanExi HS_HRAS.
    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

    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 FCSS 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 FCSS ALA-12; SER-12; VAL-12 AND ASP-13.
    46. Cited for: VARIANTS FCSS ALA-12; SER-12 AND CYS-13.
    47. Cited for: VARIANTS FCSS SER-12; CYS-12; GLU-12; ALA-12 AND ARG-117.
    48. Cited for: VARIANTS FCSS 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 FCSS ILE-58 AND VAL-146.
    51. Cited for: VARIANTS FCSS 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 FCSS 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 1, 2014
    This is version 192 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

    Similar proteinsi