UniProtKB - P01112 (RASH_HUMAN)
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Protein
GTPase HRas
Gene
HRAS
Organism
Homo sapiens (Human)
Status
Functioni
Involved in the activation of Ras protein signal transduction (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151).4 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 10 – 17 | GTP | 8 | |
Nucleotide bindingi | 57 – 61 | GTP | 5 | |
Nucleotide bindingi | 116 – 119 | GTP | 4 |
GO - Molecular functioni
- GDP binding Source: CAFA
- GTPase activity Source: WormBase
- GTP binding Source: UniProtKB
- protein C-terminus binding Source: UniProtKB
GO - Biological processi
- animal organ morphogenesis Source: ProtInc
- axon guidance Source: Reactome
- cell cycle arrest Source: BHF-UCL
- cell proliferation Source: Ensembl
- cell surface receptor signaling pathway Source: ProtInc
- cellular response to gamma radiation Source: CAFA
- cellular senescence Source: BHF-UCL
- chemotaxis Source: ProtInc
- defense response to protozoan Source: Ensembl
- endocytosis Source: Ensembl
- ephrin receptor signaling pathway Source: Reactome
- epidermal growth factor receptor signaling pathway Source: Reactome
- ERBB2 signaling pathway Source: Reactome
- Fc-epsilon receptor signaling pathway Source: Reactome
- intrinsic apoptotic signaling pathway Source: Ensembl
- leukocyte migration Source: Reactome
- MAPK cascade Source: Reactome
- mitotic cell cycle checkpoint Source: BHF-UCL
- negative regulation of cell proliferation Source: BHF-UCL
- negative regulation of gene expression Source: BHF-UCL
- negative regulation of GTPase activity Source: BHF-UCL
- negative regulation of neuron apoptotic process Source: Ensembl
- positive regulation of actin cytoskeleton reorganization Source: BHF-UCL
- positive regulation of cell migration Source: BHF-UCL
- positive regulation of cell proliferation Source: BHF-UCL
- positive regulation of DNA replication Source: BHF-UCL
- positive regulation of epithelial cell proliferation Source: BHF-UCL
- positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
- positive regulation of GTPase activity Source: BHF-UCL
- positive regulation of interferon-gamma production Source: Ensembl
- positive regulation of JNK cascade Source: BHF-UCL
- positive regulation of MAPK cascade Source: BHF-UCL
- positive regulation of MAP kinase activity Source: BHF-UCL
- positive regulation of miRNA metabolic process Source: BHF-UCL
- positive regulation of protein phosphorylation Source: BHF-UCL
- positive regulation of Ras protein signal transduction Source: Ensembl
- positive regulation of ruffle assembly Source: BHF-UCL
- positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
- positive regulation of wound healing Source: BHF-UCL
- protein heterooligomerization Source: Ensembl
- Ras protein signal transduction Source: BHF-UCL
- regulation of long-term neuronal synaptic plasticity Source: Ensembl
- response to isolation stress Source: Ensembl
- signal transduction Source: ProtInc
- stimulatory C-type lectin receptor signaling pathway Source: Reactome
- T cell receptor signaling pathway Source: Ensembl
- T-helper 1 type immune response Source: Ensembl
Keywordsi
Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-HSA-112412. SOS-mediated signalling. R-HSA-1169092. Activation of RAS in B cells. R-HSA-1236382. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants. R-HSA-1250196. SHC1 events in ERBB2 signaling. R-HSA-1250347. SHC1 events in ERBB4 signaling. R-HSA-1433557. Signaling by SCF-KIT. R-HSA-167044. Signalling to RAS. R-HSA-171007. p38MAPK events. R-HSA-179812. GRB2 events in EGFR signaling. R-HSA-180336. SHC1 events in EGFR signaling. R-HSA-186763. Downstream signal transduction. R-HSA-1963640. GRB2 events in ERBB2 signaling. R-HSA-210993. Tie2 Signaling. R-HSA-2179392. EGFR Transactivation by Gastrin. R-HSA-2424491. DAP12 signaling. R-HSA-2428933. SHC-related events triggered by IGF1R. R-HSA-2871796. FCERI mediated MAPK activation. R-HSA-375165. NCAM signaling for neurite out-growth. R-HSA-3928662. EPHB-mediated forward signaling. R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor. R-HSA-5218921. VEGFR2 mediated cell proliferation. R-HSA-5621575. CD209 (DC-SIGN) signaling. R-HSA-5637810. Constitutive Signaling by EGFRvIII. R-HSA-5654688. SHC-mediated cascade:FGFR1. R-HSA-5654693. FRS-mediated FGFR1 signaling. R-HSA-5654699. SHC-mediated cascade:FGFR2. R-HSA-5654700. FRS-mediated FGFR2 signaling. R-HSA-5654704. SHC-mediated cascade:FGFR3. R-HSA-5654706. FRS-mediated FGFR3 signaling. R-HSA-5654712. FRS-mediated FGFR4 signaling. R-HSA-5654719. SHC-mediated cascade:FGFR4. R-HSA-5655253. Signaling by FGFR2 in disease. R-HSA-5655291. Signaling by FGFR4 in disease. R-HSA-5655302. Signaling by FGFR1 in disease. R-HSA-5658442. Regulation of RAS by GAPs. R-HSA-5673000. RAF activation. R-HSA-5673001. RAF/MAP kinase cascade. R-HSA-5674135. MAP2K and MAPK activation. R-HSA-5675221. Negative regulation of MAPK pathway. R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants. R-HSA-6802948. Signaling by high-kinase activity BRAF mutants. R-HSA-6802949. Signaling by RAS mutants. R-HSA-6802952. Signaling by BRAF and RAF fusions. R-HSA-6802953. RAS signaling downstream of NF1 loss-of-function variants. R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF. R-HSA-74751. Insulin receptor signalling cascade. R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases. R-HSA-8851805. MET activates RAS signaling. R-HSA-8853334. Signaling by FGFR3 fusions in cancer. R-HSA-8853338. Signaling by FGFR3 point mutants in cancer. |
SignaLinki | P01112. |
SIGNORi | P01112. |
Names & Taxonomyi
Protein namesi | Recommended name: GTPase HRasAlternative 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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC: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
- Cytoplasm › perinuclear region
Note: Colocalizes with RACK1 to the perinuclear region.
GO - Cellular componenti
- cytoplasm Source: ProtInc
- cytosol Source: Reactome
- Golgi apparatus Source: UniProtKB
- Golgi membrane Source: UniProtKB-SubCell
- nucleus Source: UniProtKB-SubCell
- perinuclear region of cytoplasm Source: UniProtKB-SubCell
- plasma membrane Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Golgi apparatus, Membrane, NucleusPathology & Biotechi
Involvement in diseasei
Costello syndrome (CSTLO)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities.
See also OMIM:218040Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_026106 | 12 | G → A in CSTLO. 3 PublicationsCorresponds to variant dbSNP:rs104894230Ensembl. | 1 | |
Natural variantiVAR_045975 | 12 | G → C in CSTLO. 2 PublicationsCorresponds to variant dbSNP:rs104894229Ensembl. | 1 | |
Natural variantiVAR_068816 | 12 | G → D in CSTLO; severe mutation. 1 PublicationCorresponds to variant dbSNP:rs104894230Ensembl. | 1 | |
Natural variantiVAR_045976 | 12 | G → E in CSTLO. 1 Publication | 1 | |
Natural variantiVAR_006837 | 12 | G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant dbSNP:rs104894229Ensembl. | 1 | |
Natural variantiVAR_006836 | 12 | G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane. 4 PublicationsCorresponds to variant dbSNP:rs104894230Ensembl. | 1 | |
Natural variantiVAR_026107 | 13 | G → C in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894228Ensembl. | 1 | |
Natural variantiVAR_026108 | 13 | G → D in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894226Ensembl. | 1 | |
Natural variantiVAR_068818 | 37 | E → EE in CSTLO. 1 Publication | 1 | |
Natural variantiVAR_045978 | 58 | T → I in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs121917758Ensembl. | 1 | |
Natural variantiVAR_045981 | 117 | K → R in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894227Ensembl. | 1 | |
Natural variantiVAR_045982 | 146 | A → T in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894231Ensembl. | 1 | |
Natural variantiVAR_045983 | 146 | A → V in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs121917759Ensembl. | 1 |
Congenital myopathy with excess of muscle spindles (CMEMS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionVariant of Costello syndrome.
See also OMIM:218040Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_006837 | 12 | G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant dbSNP:rs104894229Ensembl. | 1 | |
Natural variantiVAR_006836 | 12 | G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane. 4 PublicationsCorresponds to variant dbSNP:rs104894230Ensembl. | 1 | |
Natural variantiVAR_045977 | 22 | Q → K in CMEMS. 1 PublicationCorresponds to variant dbSNP:rs121917757Ensembl. | 1 | |
Natural variantiVAR_045980 | 63 | E → K in CMEMS. 1 PublicationCorresponds to variant dbSNP:rs121917756Ensembl. | 1 |
Thyroid cancer, non-medullary, 2 (NMTC2)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA form of non-medullary thyroid cancer (NMTC), a cancer characterized by tumors originating from the thyroid follicular cells. NMTCs represent approximately 95% of all cases of thyroid cancer and are classified into papillary, follicular, Hurthle cell, and anaplastic neoplasms.
See also OMIM:188470Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_045979 | 61 | Q → K in NMTC2; somatic mutation; increases transformation of cultured cell lines. 2 PublicationsCorresponds to variant dbSNP:rs28933406Ensembl. | 1 |
Mutations which change positions 12, 13 or 61 activate the potential of HRAS to transform cultured cells and are implicated in a variety of human tumors.1 Publication
Bladder cancer (BLC)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences.
See also OMIM:109800Schimmelpenning-Feuerstein-Mims syndrome (SFM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis.
See also OMIM:163200Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_068817 | 13 | G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. 1 PublicationCorresponds to variant dbSNP:rs104894228Ensembl. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 17 | S → N: Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2. 2 Publications | 1 | |
Mutagenesisi | 26 | N → G: Loss of interaction with PLCE1; when associated with V-12. 1 Publication | 1 | |
Mutagenesisi | 29 | V → A: No effect on interaction with PLCE1; when associated with V-12. 1 Publication | 1 | |
Mutagenesisi | 32 | Y → F: Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12. 1 Publication | 1 | |
Mutagenesisi | 34 | P → G: No effect on interaction with PLCE1; when associated with V-12. 1 Publication | 1 | |
Mutagenesisi | 35 | T → S: Loss of interaction with PLCE1; when associated with V-12. 1 Publication | 1 | |
Mutagenesisi | 37 | E → G: No effect on interaction with PLCE1; when associated with V-12. 1 Publication | 1 | |
Mutagenesisi | 38 | D → N: No effect on interaction with PLCE1; when associated with V-12. 1 Publication | 1 | |
Mutagenesisi | 39 | S → C: No effect on interaction with PLCE1; when associated with V-12. 1 Publication | 1 | |
Mutagenesisi | 59 | A → T: Loss of GTPase activity and creation of an autophosphorylation site. | 1 | |
Mutagenesisi | 61 | Q → I: Moderately increased transformation of cultured cell lines. 1 Publication | 1 | |
Mutagenesisi | 61 | Q → V: Strongly increased transformation of cultured cell lines. 1 Publication | 1 | |
Mutagenesisi | 83 | A → T: GTP-binding activity reduced by factor of 30. 1 Publication | 1 | |
Mutagenesisi | 118 | C → S: Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange. 2 Publications | 1 | |
Mutagenesisi | 119 | D → N: Loss of GTP-binding activity. 1 Publication | 1 | |
Mutagenesisi | 144 | T → I: GTP-binding activity reduced by factor of 25. 1 Publication | 1 | |
Mutagenesisi | 164 – 165 | RQ → AV: Loss of GTP-binding activity. 1 Publication | 2 | |
Mutagenesisi | 181 | C → S: Exclusively localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-184. 2 Publications | 1 | |
Mutagenesisi | 184 | C → 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 | 1 |
Keywords - Diseasei
Disease mutation, Proto-oncogeneOrganism-specific databases
DisGeNETi | 3265. |
GeneReviewsi | HRAS. |
MalaCardsi | HRAS. |
MIMi | 109800. phenotype. 163200. phenotype. 188470. phenotype. 218040. phenotype. |
OpenTargetsi | ENSG00000174775. |
Orphaneti | 3071. Costello syndrome. 2612. Linear nevus sebaceus syndrome. 2874. Phakomatosis pigmentokeratotica. |
PharmGKBi | PA29444. |
Chemistry databases
ChEMBLi | CHEMBL2167. |
DrugBanki | DB04315. Guanosine-5'-Diphosphate. DB04137. Guanosine-5'-Triphosphate. DB03226. Trifluoroethanol. |
GuidetoPHARMACOLOGYi | 2822. |
Polymorphism and mutation databases
BioMutai | HRAS. |
DMDMi | 131869. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000042996 | 1 – 186 | GTPase HRasAdd BLAST | 186 | |
Initiator methioninei | Removed; alternate1 Publication | |||
ChainiPRO_0000326476 | 2 – 186 | GTPase HRas, N-terminally processedAdd BLAST | 185 | |
PropeptideiPRO_0000042997 | 187 – 189 | Removed in mature form | 3 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionine; in GTPase HRas; alternate1 Publication | 1 | |
Modified residuei | 2 | N-acetylthreonine; in GTPase HRas, N-terminally processed1 Publication | 1 | |
Modified residuei | 104 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 118 | S-nitrosocysteine1 Publication | 1 | |
Lipidationi | 181 | S-palmitoyl cysteine4 Publications | 1 | |
Lipidationi | 184 | S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate1 Publication | 1 | |
Lipidationi | 184 | S-palmitoyl cysteine; alternate4 Publications | 1 | |
Modified residuei | 186 | Cysteine methyl ester1 Publication | 1 | |
Lipidationi | 186 | S-farnesyl cysteine1 Publication | 1 |
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-nitrosylationProteomic databases
EPDi | P01112. |
PaxDbi | P01112. |
PeptideAtlasi | P01112. |
PRIDEi | P01112. |
PTM databases
iPTMneti | P01112. |
PhosphoSitePlusi | P01112. |
SwissPalmi | P01112. |
Expressioni
Tissue specificityi
Widely expressed.1 Publication
Gene expression databases
Bgeei | ENSG00000174775. |
CleanExi | HS_HRAS. |
ExpressionAtlasi | P01112. baseline and differential. |
Genevisiblei | P01112. HS. |
Organism-specific databases
HPAi | CAB002015. HPA049830. |
Interactioni
Subunit structurei
In its GTP-bound form interacts with PLCE1 (PubMed:11022048). Interacts with TBC1D10C (PubMed:17230191). Interacts with RGL3 (By similarity). Interacts with HSPD1 (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (By similarity). Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) (By similarity). Forms a signaling complex with RASGRP1 and DGKZ (PubMed:11257115). Interacts with RASSF5 (PubMed:18596699). Interacts with PDE6D (PubMed:11980706). Interacts with IKZF3 (PubMed:10369681). Interacts with RACK1 (PubMed:14500341). Interacts with PIK3CG; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (By similarity). Interacts with RAPGEF2 (PubMed:10608844, PubMed:11598133).By similarity10 Publications
Binary interactionsi
GO - Molecular functioni
- protein C-terminus binding Source: UniProtKB
Protein-protein interaction databases
BioGridi | 109501. 99 interactors. |
DIPi | DIP-1050N. |
ELMi | P01112. |
IntActi | P01112. 51 interactors. |
MINTi | MINT-5002362. |
STRINGi | 9606.ENSP00000309845. |
Chemistry databases
BindingDBi | P01112. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 3 – 11 | Combined sources | 9 | |
Beta strandi | 12 – 14 | Combined sources | 3 | |
Helixi | 16 – 25 | Combined sources | 10 | |
Beta strandi | 27 – 31 | Combined sources | 5 | |
Beta strandi | 34 – 37 | Combined sources | 4 | |
Beta strandi | 38 – 46 | Combined sources | 9 | |
Beta strandi | 49 – 57 | Combined sources | 9 | |
Beta strandi | 60 – 63 | Combined sources | 4 | |
Helixi | 66 – 74 | Combined sources | 9 | |
Beta strandi | 76 – 83 | Combined sources | 8 | |
Turni | 84 – 86 | Combined sources | 3 | |
Helixi | 87 – 104 | Combined sources | 18 | |
Beta strandi | 105 – 107 | Combined sources | 3 | |
Beta strandi | 111 – 116 | Combined sources | 6 | |
Beta strandi | 120 – 122 | Combined sources | 3 | |
Helixi | 127 – 136 | Combined sources | 10 | |
Beta strandi | 141 – 144 | Combined sources | 4 | |
Turni | 146 – 148 | Combined sources | 3 | |
Helixi | 152 – 164 | Combined sources | 13 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
2N42 | NMR | - | A | 1-166 | [»] | |
2N46 | 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 | [»] | |
4RSG | neutron diffraction | 1.91 | A | 1-166 | [»] | |
4URU | X-ray | 2.83 | R | 1-166 | [»] | |
4URV | X-ray | 2.58 | R | 1-166 | [»] | |
4URW | X-ray | 2.76 | R | 1-166 | [»] | |
4URX | X-ray | 2.49 | R | 1-166 | [»] | |
4URY | X-ray | 2.47 | R | 1-166 | [»] | |
4URZ | X-ray | 2.24 | R | 1-166 | [»] | |
4US0 | X-ray | 2.17 | R | 1-166 | [»] | |
4US1 | X-ray | 2.65 | R | 1-166 | [»] | |
4US2 | X-ray | 2.48 | R | 1-166 | [»] | |
4XVQ | X-ray | 1.89 | A | 1-166 | [»] | |
4XVR | X-ray | 2.03 | A | 1-166 | [»] | |
521P | X-ray | 2.60 | A | 1-166 | [»] | |
5B2Z | X-ray | 1.56 | A | 1-166 | [»] | |
5B30 | X-ray | 1.60 | A | 1-166 | [»] | |
5E95 | X-ray | 1.40 | 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. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P01112. |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 166 – 185 | Hypervariable regionAdd BLAST | 20 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 32 – 40 | Effector region | 9 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0395. Eukaryota. COG1100. LUCA. |
GeneTreei | ENSGT00860000133672. |
HOGENOMi | HOG000233973. |
HOVERGENi | HBG009351. |
InParanoidi | P01112. |
KOi | K02833. |
OMAi | DCMNCKC. |
OrthoDBi | EOG091G0UAU. |
PhylomeDBi | P01112. |
TreeFami | TF312796. |
Family and domain databases
InterProi | View protein in InterPro IPR027417. P-loop_NTPase. IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR020849. Small_GTPase_Ras. |
PANTHERi | PTHR24070. PTHR24070. 1 hit. |
Pfami | View protein in Pfam PF00071. Ras. 1 hit. |
SUPFAMi | SSF52540. SSF52540. 1 hit. |
TIGRFAMsi | TIGR00231. small_GTP. 1 hit. |
PROSITEi | View protein in PROSITE PS51421. RAS. 1 hit. |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basket
Isoform 1 (identifier: P01112-1) [UniParc]FASTAAdd to basket
Also known as: H-Ras4A, p21
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
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
Mass spectrometryi
Molecular mass is 6253±2 Da from positions 112 - 166. Determined by ESI. Includes one nitric oxide molecule.1 Publication
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_026106 | 12 | G → A in CSTLO. 3 PublicationsCorresponds to variant dbSNP:rs104894230Ensembl. | 1 | |
Natural variantiVAR_045975 | 12 | G → C in CSTLO. 2 PublicationsCorresponds to variant dbSNP:rs104894229Ensembl. | 1 | |
Natural variantiVAR_068816 | 12 | G → D in CSTLO; severe mutation. 1 PublicationCorresponds to variant dbSNP:rs104894230Ensembl. | 1 | |
Natural variantiVAR_045976 | 12 | G → E in CSTLO. 1 Publication | 1 | |
Natural variantiVAR_006837 | 12 | G → S in CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma. 6 PublicationsCorresponds to variant dbSNP:rs104894229Ensembl. | 1 | |
Natural variantiVAR_006836 | 12 | G → V in CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane. 4 PublicationsCorresponds to variant dbSNP:rs104894230Ensembl. | 1 | |
Natural variantiVAR_026107 | 13 | G → C in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894228Ensembl. | 1 | |
Natural variantiVAR_026108 | 13 | G → D in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894226Ensembl. | 1 | |
Natural variantiVAR_068817 | 13 | G → R in SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. 1 PublicationCorresponds to variant dbSNP:rs104894228Ensembl. | 1 | |
Natural variantiVAR_045977 | 22 | Q → K in CMEMS. 1 PublicationCorresponds to variant dbSNP:rs121917757Ensembl. | 1 | |
Natural variantiVAR_068818 | 37 | E → EE in CSTLO. 1 Publication | 1 | |
Natural variantiVAR_045978 | 58 | T → I in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs121917758Ensembl. | 1 | |
Natural variantiVAR_045979 | 61 | Q → K in NMTC2; somatic mutation; increases transformation of cultured cell lines. 2 PublicationsCorresponds to variant dbSNP:rs28933406Ensembl. | 1 | |
Natural variantiVAR_006838 | 61 | Q → L in melanoma; strongly reduced GTP hydrolysis in the presence of RAF1; increases transformation of cultured cell lines. 1 PublicationCorresponds to variant dbSNP:rs121913233Ensembl. | 1 | |
Natural variantiVAR_045980 | 63 | E → K in CMEMS. 1 PublicationCorresponds to variant dbSNP:rs121917756Ensembl. | 1 | |
Natural variantiVAR_078259 | 89 | S → C Found in a patient with severe fetal hydrops and pleural effusion; unknown pathological significance; decreased activation of Ras protein signal transduction. 1 PublicationCorresponds to variant dbSNP:rs755322824Ensembl. | 1 | |
Natural variantiVAR_045981 | 117 | K → R in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894227Ensembl. | 1 | |
Natural variantiVAR_045982 | 146 | A → T in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs104894231Ensembl. | 1 | |
Natural variantiVAR_045983 | 146 | A → V in CSTLO. 1 PublicationCorresponds to variant dbSNP:rs121917759Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_041597 | 152 – 189 | VEDAF…KCVLS → SRSGSSSSSGTLWDPPGPM in isoform 2. 2 PublicationsAdd BLAST | 38 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J00277 Genomic DNA. Translation: AAB02605.1. AJ437024 mRNA. Translation: CAD24594.1. AF493916 mRNA. Translation: AAM12630.1. CR536579 mRNA. Translation: CAG38816.1. CR542271 mRNA. Translation: CAG47067.1. BT019421 mRNA. Translation: AAV38228.1. EF015887 Genomic DNA. Translation: ABI97389.1. AB451336 mRNA. Translation: BAG70150.1. AB451485 mRNA. Translation: BAG70299.1. CH471158 Genomic DNA. Translation: EAX02337.1. CH471158 Genomic DNA. Translation: EAX02338.1. BC006499 mRNA. Translation: AAH06499.1. BC095471 mRNA. Translation: AAH95471.1. M17232 Genomic DNA. Translation: AAA35685.1. |
CCDSi | CCDS7698.1. [P01112-1] CCDS7699.1. [P01112-2] |
PIRi | A93299. TVHUH. |
RefSeqi | NP_001123914.1. NM_001130442.2. [P01112-1] NP_001304983.1. NM_001318054.1. NP_005334.1. NM_005343.3. [P01112-1] NP_789765.1. NM_176795.4. [P01112-2] |
UniGenei | Hs.37003. |
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | RASH_HUMAN | |
Accessioni | P01112Primary (citable) accession number: P01112 Secondary accession number(s): B5BUA0 Q9UCE2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 21, 1986 | |
Last modified: | August 30, 2017 | |
This is version 225 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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 proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families