GTPase HRas (HRAS)
The protein contains 189 amino acids for an estimated molecular weight of 21298 Da.
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). (updated: Dec. 20, 2017)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
Biological Process
Actin cytoskeleton organization
Activation of MAPKK activity
Animal organ morphogenesis
Axon guidance
Blood coagulation
Cell cycle arrest
Cell population proliferation
Cell surface receptor signaling pathway
Cellular response to gamma radiation
Cellular senescence
Chemical synaptic transmission
Chemotaxis
Defense response to protozoan
Endocytosis
Ephrin receptor signaling pathway
Epidermal growth factor receptor signaling pathway
Epithelial tube branching involved in lung morphogenesis
ERBB2 signaling pathway
Fc-epsilon receptor signaling pathway
Fibroblast growth factor receptor signaling pathway
Innate immune response
Insulin receptor signaling pathway
Intrinsic apoptotic signaling pathway
Leukocyte migration
Liver development
MAPK cascade
Mitotic cell cycle checkpoint signaling
Negative regulation of cell differentiation
Negative regulation of cell population proliferation
Negative regulation of gene expression
Negative regulation of GTPase activity
Negative regulation of neuron apoptotic process
Neurotrophin TRK receptor signaling pathway
Positive regulation of actin cytoskeleton reorganization
Positive regulation of cell migration
Positive regulation of cell population proliferation
Positive regulation of DNA replication
Positive regulation of epithelial cell proliferation
Positive regulation of ERK1 and ERK2 cascade
Positive regulation of GTPase activity
Positive regulation of interferon-gamma production
Positive regulation of JNK cascade
Positive regulation of MAP kinase activity
Positive regulation of MAPK cascade
Positive regulation of miRNA metabolic process
Positive regulation of phospholipase C activity
Positive regulation of protein phosphorylation
Positive regulation of protein targeting to membrane
Positive regulation of Rac protein signal transduction
Positive regulation of Ras protein signal transduction
Positive regulation of ruffle assembly
Positive regulation of transcription by RNA polymerase II
Positive regulation of wound healing
Protein heterooligomerization
Ras protein signal transduction
Regulation of long-term neuronal synaptic plasticity
Regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
Regulation of synaptic transmission, GABAergic
Response to isolation stress
Signal transduction
Small GTPase mediated signal transduction
Social behavior
Stimulatory C-type lectin receptor signaling pathway
Striated muscle cell differentiation
T cell receptor signaling pathway
T-helper 1 type immune response
Vascular endothelial growth factor receptor signaling pathway
Visual learning
The reference OMIM entry for this protein is 109800
Bladder cancer
A number sign (#) is used with this entry because bladder cancer is a complex disorder with both genetic and environmental influences. Somatic mutations in several genes, e.g., HRAS (190020), KRAS2 (190070), RB1 (614041), and FGFR3 (134934), have been implicated in bladder carcinogenesis. See Bishop (1982) for a discussion of oncogenes.
CLINICAL FEATURES
Patients with cancer of the urinary bladder often present with multiple tumors appearing at different times and at different sites in the bladder. This observation had been attributed to a 'field defect' in the bladder that allowed the independent transformation of epithelial cells at a number of sites. Sidransky et al. (1992) tested this hypothesis with molecular genetic techniques and concluded that in fact multiple bladder tumors are of clonal origin. A number of bladder tumors can arise from the uncontrolled spread of a single transformed cell. These tumors can then grow independently with variable subsequent genetic alterations. Dyrskjot et al. (2003) reported the identification of clinically relevant subclasses of bladder carcinoma using expression microarray analysis of 40 well-characterized bladder tumors. Gene expression profiles characterizing each stage and subtype identified their biologic properties, producing potential targets for therapy.INHERITANCE
Fraumeni and Thomas (1967) observed affected father and 3 sons. McKusick (1972) encountered 2 instances of affected father and son at the Johns Hopkins Hospital. McCullough et al. (1975) found transitional cell carcinoma (TCC) in 6 persons in 3 sibships of 2 generations of a kindred. In a review of case reports and epidemiologic studies in the literature, Kiemeney and Schoenberg (1996) concluded that first-degree relatives have an increased risk for TCC by a factor of 2. Familial clustering of smoking did not appear to be the cause of this increased risk. In Iceland, Kiemeney et al. (1997) studied the first- to third-degree relatives of 190 patients with bladder, ureter, or renal pelvis TCC diagnosed between 1983 and 1992. In 41 of the 190 pedigrees, at least 1 relative had TCC of the urinary tract. Of the probands, 38 had only 1 and 3 had 2 affected relatives. The prevalence of family history of TCC was 3% in first-degree and 10% in first- or second-degree relatives. The risk of TCC among all relatives was slightly elevated, the observed-to-expected ratio being greater among second- and third-degree relatives than among first-degree relatives. Kiemeney et al. (1997) concluded that the greater risk among distant relatives argues against the existence of a hereditary subtype of bladder TCC, at least in the founder population of Iceland.MAPPING
Goldfarb et al. (1982) studied the DNA from T24, a cell line derived from a human bladder carcinoma, which can induce the morphologic transformation of nonmalignant cells. The gene responsible for this transformation was cloned by techniques of gene rescue: it was shown to be human in origin and less than 5 kb long. By Southern blot analysis of human-rodent hybrid cell DNA, de Martinville et al. (1983) found that the cellular homolog of the transforming DNA sequence isolated from the bladder carcinoma line EJ is located on the short arm of chromosome 11, which contains sequences homologous to the HRAS (190020) oncogene. No evidence of gene amplification was found. These workers also found karyologically 'a complex rearrangement of the short arm in two of ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for HRAS
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 109800 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed