| + |
HRAS | up-regulates activity 
phosphorylation
|
GATA2 |
0.367 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259945 |
Ser192 |
PSTTGAAsPASSSAG |
Homo sapiens |
|
| pmid |
sentence |
| 25056917 |
Oncogenic Ras enhanced S192-dependent GATA-2 phosphorylation, nuclear foci localization, and transcriptional activation. These studies define a mechanism that controls a key regulator of hematopoiesis and a dual mode of impairing GATA-2-dependent genetic networks: mutational disruption of chromatin occupancy yielding insufficient GATA-2, and oncogenic Ras-mediated amplification of GATA-2 activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | HaematopoiesisTranscriptionalControl |
| + |
HRAS | up-regulates activity 
phosphorylation
|
JUN |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236682 |
Ser63 |
KNSDLLTsPDVGLLK |
Rattus norvegicus |
Fibroblast |
| pmid |
sentence |
| 1749429 |
Expression of oncogenic ha-ras augments transactivation by c-jun and stimulates its phosphorylation. Here we describe the mapping of the ha-ras-responsive phosphorylation sites to serines 63 and 73 of c-jun. Site-directed mutagenesis indicates that phosphorylation of these serines is essential for stimulation of c-jun activity and for cooperation with ha-ras in ocogenic transformation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235522 |
Ser63 |
KNSDLLTsPDVGLLK |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 12169099 |
c-Jun was first shown to be phosphorylated in its transactivation domain (Ser-63 and Ser-73) by ERKs and p54-JNK. This is consistent with other studies which show that PD98059 inhibits up-regulation of c-Jun protein in Ras-transformed NIH-3T3 cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236686 |
Ser73 |
VGLLKLAsPELERLI |
Rattus norvegicus |
Fibroblast |
| pmid |
sentence |
| 1749429 |
Expression of oncogenic ha-ras augments transactivation by c-jun and stimulates its phosphorylation. Here we describe the mapping of the ha-ras-responsive phosphorylation sites to serines 63 and 73 of c-jun. Site-directed mutagenesis indicates that phosphorylation of these serines is essential for stimulation of c-jun activity and for cooperation with ha-ras in ocogenic transformation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235526 |
Ser73 |
VGLLKLAsPELERLI |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 12169099 |
c-Jun was first shown to be phosphorylated in its transactivation domain (Ser-63 and Ser-73) by ERKs and p54-JNK. This is consistent with other studies which show that PD98059 inhibits up-regulation of c-Jun protein in Ras-transformed NIH-3T3 cells |
|
| Publications: |
4 |
Organism: |
Rattus Norvegicus, Mus Musculus |
| Pathways: | HaematopoiesisTranscriptionalControl, EGFR Signaling, Glioblastoma Multiforme, Insulin Signaling |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
HRAS |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252094 |
Tyr32 |
QNHFVDEyDPTIEDS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26617336 |
Here we identify SHP2 as the ubiquitously expressed tyrosine phosphatase that preferentially binds to and dephosphorylates Ras to increase its association with Raf and activate downstream proliferative Ras/ERK/MAPK signalling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, Noonan syndrome |
| + |
SRC | down-regulates activity 
phosphorylation
|
HRAS |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252093 |
Tyr32 |
QNHFVDEyDPTIEDS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25157176 |
Src binds to and phosphorylates GTP-, but not GDP-, loaded Ras on a conserved Y32 residue within the switch I region in vitro and that in vivo, Ras-Y32 phosphorylation markedly reduces the binding to effector Raf and concomitantly increases binding to GTPase-activating proteins and the rate of GTP hydrolysis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, Integrin Signaling |
| + |
RAPGEF6 | up-regulates
guanine nucleotide exchange factor
|
HRAS |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183796 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19201597 |
Gefs catalyse the transition from gdp-bound, inactive ras to gtp-bound, active ras. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HRAS | up-regulates
binding
|
RAF1 |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236656 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21779497 |
The first RAS effector pathway to be identified was the RAF-MEK-ERK pathway. This pathway is an essential, shared element of mitogenic signaling involving tyrosine kinase receptors, leading to a wide range of cellular responses, including growth, differentiation, inflammation, and apoptosis.23 The RAF family of proteins (Raf-1, A-Raf, and B-Raf) is serine/threonine kinases that bind to the effector region of RAS-GTP, thus inducing translocation of the protein to the plasma membrane. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235786 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9020159 |
We have examined whether the other two members of the Raf family, A-Raf and B-Raf, are regulated in a similar way to Raf-1. A-Raf behaves like Raf-1, being weakly activated by oncogenic Ras more strongly activated by oncogenic Src, and these signals synergize to give maximal activation. B-Raf by contrast is strongly activated by oncogenic Ras alone and is not activated by oncogenic Src. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Insulin Signaling, Integrin Signaling, Noonan syndrome, Oxytocin signaling |
| + |
HRAS | up-regulates
binding
|
BRAF |
0.873 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160043 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18098337 |
BRAF kinase is a downstream target of KRAS and activates the MAPK pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235478 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 7706312 |
Association of B-Raf with immobilized Ras occurred independently of prior stimulation of cells with serum, suggesting that primarily the production of GTP-Ras by mitogen stimulation is critical for the formation of B-Raf_GTP-Ras complexes. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | EGFR Signaling, ErbB receptors in cancer, Glioblastoma Multiforme, Hepatocellular Tumor, Noonan syndrome, Non-small-cell lung cancer (NSCLC), PI3K/AKT Signaling, Rett syndrome, RTKs in cancer, T cell activation, VEGF Signaling |
| + |
GOLGA7 | up-regulates activity
palmitoylation
|
HRAS |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261351 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16000296 |
Covalent lipid modifications mediate the membrane attachment and biological activity of Ras proteins. All Ras isoforms are farnesylated and carboxyl-methylated at the terminal cysteine; H-Ras and N-Ras are further modified by palmitoylation. Here we report that H- and N-Ras are palmitoylated by a human protein palmitoyltransferase encoded by the ZDHHC9 and GCP16 genes. DHHC9 is an integral membrane protein that contains a DHHC cysteine-rich domain. GCP16 encodes a Golgi-localized membrane protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FNTB | up-regulates activity
|
HRAS |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242565 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24294527 |
Major investments have been made to target Ras through indirect routes. Inhibition of farnesyl transferase to block Ras maturation has failed in large clinical trials. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NF1 | down-regulates activity
, gtpase-activating protein
|
HRAS |
0.807 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256067 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19777070 |
NF1 negatively regulates Ras as an exchangefactor converting Ras-GTP to Ras-GDP by its GTPase-activating (Ras-GAP) domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-204357 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24431436 |
Nf1encodes neurofibromin, a protein with multiple functions including ras inactivation (ras gtpase-activating protein or rasgap) and adenylyl cyclase (ac) activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glioblastoma Multiforme |
| + |
PLCE1 | up-regulates
guanine nucleotide exchange factor
|
HRAS |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82859 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11022047 |
The presence of a rasgef motif in the n terminus of plcepsilon suggests that plcepsilon can activate ras by acting as an exchange factor by promoting the exchange of gtp for bound gdp. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Oxytocin signaling |
| + |
DAB2IP | down-regulates activity
gtpase-activating protein
|
HRAS |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254745 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27858941 |
The GAP domain of DAB2IP is homologous to other Ras-GAPs, such as GAP120 and neurofibromin (NF1), and can stimulate the GTPase activity of RAS proteins both in vitro and in cancer cell lines. DAB2IP is able to stimulate in vitro and in vivo the GTPase activity of RAS proteins (H-Ras, K-Ras, and N-Ras) facilitating GTP hydrolysis to GDP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RASA1 | down-regulates
binding
|
HRAS |
0.84 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-49477 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9219684 |
The three-dimensional structure of the complex between human h-ras bound to guanosine diphosphate and the guanosine triphosphatase (gtpase)-activating domain of the human gtpase-activating protein p120gap (gap-334) in the presence of aluminum fluoride was solved at a resolution of 2.5 angstroms. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-68990 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10394594 |
The Ras protein sits at the center of a many-tiered cascade of molecular interactions. Most of the proteins along this cascade are activated by phosphorylation, but Ras uses a bound guanine nucleotide to toggle between its on and off states. Ras hydrolyzes GTP to GDP fairly quickly, turning itself off, and a collection of GTPase-activating proteins (GAPs) speed up the processthe complex between human h-ras bound to guanosine diphosphate and the guanosine triphosphatase (gtpase)-activating domain of the human gtpase-activating protein p120gap (gap-334) in the presence of aluminum fluoride was solved. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glioblastoma Multiforme |
| + |
MVD | up-regulates quantity by stabilization
|
HRAS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265888 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12646231 |
An overexpression of mot-2 resulted in reduced level of Ras and phosphorylated ERK2. These were rescued by co-expression of MPD from an exogenous promoter demonstrating a functional link between mot-2, MPD, and Ras. Ras and its oncogenic forms act as key players in controlling proliferation of normal and cancerous cells. Assigning mot-2 upstream of p21Ras offers an important mechanism for influence over cell proliferation. Therefore, we ra tionaled to investigate if overexpression of MPD could affect the steady state levels of Ras by affecting its prenylationTransient transfections of MPD-myc in COS 7 cells resulted in higher stable levels of Ras as compared to the untransfected cells (Fig. 3A, compare lanes 4 and 8 and Fig. 3B) |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
RAPGEF5 | up-regulates
guanine nucleotide exchange factor
|
HRAS |
0.488 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183732 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19201597 |
Gefs catalyse the transition from gdp-bound, inactive ras to gtp-bound, active ras. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GNAQ | up-regulates
binding
|
HRAS |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-50104 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9235901 |
Galfaq/11 subunits also activate p21ras |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Oxytocin signaling |
| + |
RASGEF1C | up-regulates
binding
|
HRAS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161505 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19201597 |
Gefs catalyse the transition from gdp-bound, inactive ras to gtp-bound, active ras. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBIAD1 | down-regulates activity
binding
|
HRAS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256206 |
|
|
Homo sapiens |
Urinary Bladder Cancer Cell |
| pmid |
sentence |
| 30518913 |
This study show that UBIAD1 interacts with H-Ras, retains H-Ras in the Golgi apparatus, prevents H-Ras trafficking from the Golgi apparatus to the plasma membrane, blocks the aberrant activation of Ras/MAPK signaling, and inhibits the proliferation of bladder cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOS2 | up-regulates
guanine nucleotide exchange factor
|
HRAS |
0.778 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175262 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21779497 |
Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIN1 | up-regulates
binding
|
HRAS |
0.617 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11784866 |
We demonstrate that the ras effector protein rin1 binds to activated ras with an affinity (k(d), 22 nm) similar to that observed for raf1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RASGEF1A | up-regulates
binding
|
HRAS |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183823 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19201597 |
Gefs catalyse the transition from gdp-bound, inactive ras to gtp-bound, active ras. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HRAS | up-regulates activity
binding
|
PIK3CA |
0.922 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236443 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8052307 |
In vivo, dominant negative ras mutant n17 inhibits growth factor induced production of 3' phosphorylated phosphoinositides in pc12 cells, and transfection of ras, but not raf, into cos cells results in a large elevation in the level of these lipids. Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. it was also described that ras interacts with pi3k in a direct manner. lysine residue 227 is essential for the interaction of ras with pi3k |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | EGFR Signaling, Glioblastoma Multiforme |
| + |
SOS1 | up-regulates activity
guanine nucleotide exchange factor
|
HRAS |
0.886 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39237 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23132018 |
The enhancement of H-Ras GTP levels induced by oncogenic K-Ras was abrogated when the expression of endogenous Sos was suppressed, implicating Sos as an essential intermediate in the cross talk between oncogenic K-Ras and WT H-Ras. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59472 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23132018 |
The enhancement of H-Ras GTP levels induced by oncogenic K-Ras was abrogated when the expression of endogenous Sos was suppressed, implicating Sos as an essential intermediate in the cross talk between oncogenic K-Ras and WT H-Ras. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, ErbB receptors in cancer, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Integrin Signaling, Noonan syndrome, Non-small-cell lung cancer (NSCLC), PI3K/AKT Signaling, Rett syndrome, RTKs in cancer, T cell activation, VEGF Signaling |
| + |
HRAS | up-regulates
binding
|
ARAF |
0.83 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175183 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21779497 |
The raf family of proteins (raf-1, a-raf, and b-raf) is serine/threonine kinases that bind to the effector region of ras-gtp, thus inducing translocation of the protein to the plasma membrane. Once there, raf proteins are activated and phosphorylated by different protein kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling |
| + |
RASGEF1B | up-regulates
binding
|
HRAS |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183832 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19201597 |
Gefs catalyse the transition from gdp-bound, inactive ras to gtp-bound, active ras. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HRAS | up-regulates activity
binding
|
PI3K |
0.839 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252689 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8052307 |
In vivo, dominant negative ras mutant n17 inhibits growth factor induced production of 3' phosphorylated phosphoinositides in pc12 cells, and transfection of ras, but not raf, into cos cells results in a large elevation in the level of these lipids. Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. it was also described that ras interacts with pi3k in a direct manner. lysine residue 227 is essential for the interaction of ras with pi3k |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | ErbB receptors in cancer, Hepatocellular Tumor, Integrin Signaling, Non-small-cell lung cancer (NSCLC), PI3K/AKT Signaling, RTKs in cancer, T cell activation, VEGF Signaling |
| + |
HRAS | up-regulates
binding
|
PIK3CG |
0.81 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59816 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9727023 |
Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. it was also described that ras interacts with pi3k in a direct manner. lysine residue 227 is essential for the interaction of ras with pi3k we show here, however, that in vivo there are marked quantitative differences in the ability of ki- and ha-ras to activate raf-1 and phosphoinositide 3 kinase. the mechanism of raf-1 activation is complex, but it is clear that one important role of ras is to recruit raf-1 to the plasma membrane where a series of events is initiated that ultimately leads to full raf-1 activation. These events include tyrosine, serine, and threonine phosphorylation plus interactions with ras, phospholipids, 14-3-3 proteins and their associated proteins, and possibly dimerization. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175195 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21779497 |
Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. it was also described that ras interacts with pi3k in a direct manner. lysine residue 227 is essential for the interaction of ras with pi3k we show here, however, that in vivo there are marked quantitative differences in the ability of ki- and ha-ras to activate raf-1 and phosphoinositide 3 kinase. the mechanism of raf-1 activation is complex, but it is clear that one important role of ras is to recruit raf-1 to the plasma membrane where a series of events is initiated that ultimately leads to full raf-1 activation. These events include tyrosine, serine, and threonine phosphorylation plus interactions with ras, phospholipids, 14-3-3 proteins and their associated proteins, and possibly dimerization. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HRAS | up-regulates activity
binding
|
BRAF |
0.873 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147327 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21779497 |
The raf family of proteins (raf-1, a-raf, and b-raf) is serine/threonine kinases that bind to the effector region of ras-gtp, thus inducing translocation of the protein to the plasma membrane. Once there, raf proteins are activated and phosphorylated by different protein kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, ErbB receptors in cancer, Glioblastoma Multiforme, Hepatocellular Tumor, Noonan syndrome, Non-small-cell lung cancer (NSCLC), PI3K/AKT Signaling, Rett syndrome, RTKs in cancer, T cell activation, VEGF Signaling |
| + |
ZDHHC9 | up-regulates activity
palmitoylation
|
HRAS |
0.452 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261352 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16000296 |
Covalent lipid modifications mediate the membrane attachment and biological activity of Ras proteins. All Ras isoforms are farnesylated and carboxyl-methylated at the terminal cysteine; H-Ras and N-Ras are further modified by palmitoylation. Here we report that H- and N-Ras are palmitoylated by a human protein palmitoyltransferase encoded by the ZDHHC9 and GCP16 genes. DHHC9 is an integral membrane protein that contains a DHHC cysteine-rich domain. GCP16 encodes a Golgi-localized membrane protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HRAS | up-regulates
binding
|
PIK3CA |
0.922 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-35878 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8052307 |
In vivo, dominant negative ras mutant n17 inhibits growth factor induced production of 3' phosphorylated phosphoinositides in pc12 cells, and transfection of ras, but not raf, into cos cells results in a large elevation in the level of these lipids. Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. it was also described that ras interacts with pi3k in a direct manner. lysine residue 227 is essential for the interaction of ras with pi3k |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, Glioblastoma Multiforme |
| + |
HRAS | up-regulates activity
binding
|
PIK3CB |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175189 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21779497 |
Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. it was also described that ras interacts with pi3k in a direct manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Insulin Signaling |
| + |
NIBAN2 | up-regulates activity
binding
|
HRAS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273659 |
|
|
Homo sapiens |
U-251MG Cell |
| pmid |
sentence |
| 26721396 |
EGFR phosphorylates FAM129B, resulting in binding of phosphorylated FAM129B to H-Ras and reduced the association of p120-RasGAP with H-Ras, thereby enhancing H-Ras activation for ERK1/2-dependent β-catenin transactivation for enhanced Warburg effect, tumor cell proliferation, and brain tumorigenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HRAS | up-regulates
binding
|
PIK3CD |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175192 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21779497 |
Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. it was also described that ras interacts with pi3k in a direct manner. lysine residue 227 is essential for the interaction of ras with pi3k |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FNTA | up-regulates activity
|
HRAS |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242568 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24294527 |
Major investments have been made to target Ras through indirect routes. Inhibition of farnesyl transferase to block Ras maturation has failed in large clinical trials. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
HRAS
- 
- 