Gene Symbol | RRAGC |
Entrez ID | 64121 |
Uniprot ID | Q9HB90 |
Description | Ras-related GTP binding C |
Chromosomal Location | chr1: 38,838,198-38,859,823 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0006351 |
transcription, DNA-templated |
The cellular synthesis of RNA on a template of DNA. |
NAS |
BP |
GO:0006915 |
apoptotic process |
A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
NAS |
BP |
GO:0007050 |
cell cycle arrest |
A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M). |
TAS |
BP |
GO:0007264 |
small GTPase mediated signal transduction |
Any series of molecular signals in which a small monomeric GTPase relays one or more of the signals. |
TAS |
BP |
GO:0008380 |
RNA splicing |
The process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA. |
NAS |
BP |
GO:0010506 |
regulation of autophagy |
Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. |
IBA |
BP |
GO:0016049 |
cell growth |
The process in which a cell irreversibly increases in size over time by accretion and biosynthetic production of matter similar to that already present. |
NAS |
BP |
GO:0016236 |
macroautophagy |
The major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane-bounded autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane-bounded structure. Autophagosomes then fuse with a lysosome (or vacuole) releasing single-membrane-bounded autophagic bodies that are then degraded within the lysosome (or vacuole). Though once thought to be a purely non-selective process, it appears that some types of macroautophagy, e.g. macropexophagy, macromitophagy, may involve selective targeting of the targets to be degraded. |
TAS |
BP |
GO:0032006 |
regulation of TOR signaling |
Any process that modulates the frequency, rate or extent of TOR signaling. |
IGI |
BP |
GO:0032008 |
positive regulation of TOR signaling |
Any process that activates or increases the frequency, rate or extent of TOR signaling. |
IBA |
BP |
GO:0034198 |
cellular response to amino acid starvation |
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of amino acids. |
IGI |
BP |
GO:0034613 |
cellular protein localization |
Any process in which a protein is transported to, and/or maintained in, a specific location at the level of a cell. Localization at the cellular level encompasses movement within the cell, from within the cell to the cell surface, or from one location to another at the surface of a cell. |
ISS |
BP |
GO:0043200 |
response to amino acid |
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an amino acid stimulus. An amino acid is a carboxylic acids containing one or more amino groups. |
IMP |
BP |
GO:0071230 |
cellular response to amino acid stimulus |
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an amino acid stimulus. An amino acid is a carboxylic acids containing one or more amino groups. |
IBA|ISS |
BP |
GO:1903432 |
regulation of TORC1 signaling |
Any process that modulates the frequency, rate or extent of TORC1 signaling. |
IMP |
CC |
GO:0005634 |
nucleus |
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
IDA |
CC |
GO:0005737 |
cytoplasm |
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
IDA |
CC |
GO:0005764 |
lysosome |
A small lytic vacuole that has cell cycle-independent morphology and is found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. |
IDA |
CC |
GO:0005829 |
cytosol |
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
TAS |
CC |
GO:0034448 |
EGO complex |
A vacuolar membrane-associated protein complex that is required for activation of microautophagy during exit from rapamycin-induced growth arrest. In budding yeast, S. cerevisiae, this complex includes Gtr1p, Gtr2p, Meh1p, and Slm4p. |
IBA |
CC |
GO:0043231 |
intracellular membrane-bounded organelle |
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
IDA |
CC |
GO:1990131 |
Gtr1-Gtr2 GTPase complex |
A heterodimer GTPase complex. In S. cerevisiae, this complex contains Gtr1p and Gtr2p proteins. |
IBA |
MF |
GO:0000287 |
magnesium ion binding |
Interacting selectively and non-covalently with magnesium (Mg) ions. |
NAS |
MF |
GO:0003924 |
GTPase activity |
Catalysis of the reaction: GTP + H2O = GDP + phosphate. |
IDA |
MF |
GO:0005515 |
protein binding |
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). |
IPI |
MF |
GO:0005525 |
GTP binding |
Interacting selectively and non-covalently with GTP, guanosine triphosphate. |
IDA|IMP |
MF |
GO:0019003 |
GDP binding |
Interacting selectively and non-covalently with GDP, guanosine 5'-diphosphate. |
IDA |
MF |
GO:0046982 |
protein heterodimerization activity |
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer. |
IPI |
Domain ID | Description |
---|---|
IPR006762 |
Gtr1/RagA G protein |
IPR027417 |
P-loop containing nucleoside triphosphate hydrolase |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa04140 |
Autophagy - animal |
KEGG |
hsa04150 |
mTOR signaling pathway |
KEGG |
WP1471 |
Target Of Rapamycin (TOR) Signaling |
WikiPathways |
Tissue | Cell Type |
---|---|
bone marrow |
hematopoietic cells |
bronchus |
respiratory epithelial cells |
caudate |
glial cells |
cerebellum |
cells in molecular layer |
cerebral cortex |
glial cells |
colon |
endothelial cells |
duodenum |
glandular cells |
gallbladder |
glandular cells |
heart muscle |
myocytes |
hippocampus |
glial cells |
nasopharynx |
respiratory epithelial cells |
pancreas |
exocrine glandular cells |
placenta |
trophoblastic cells |
salivary gland |
glandular cells |
skin |
fibroblasts |
skin |
keratinocytes |
skin |
Langerhans |
skin |
melanocytes |
small intestine |
glandular cells |
soft tissue |
fibroblasts |
soft tissue |
peripheral nerve |
stomach |
glandular cells |
testis |
cells in seminiferous ducts |
thyroid gland |
glandular cells |
urinary bladder |
urothelial cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
22617121 |
Ouandaogo et al. |
2012 |
Differences in transcriptomic profiles of human cumulus cells isolated from oocytes at GV, MI and MII stages after in vivo andin vitro oocyte maturation |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
ATP6V1A |
523 |
P38606 |
0.63 |
TSC1 |
7248 |
Q92574 |
0.63 |
WNT2 |
7472 |
P09544 |
0.63 |
ATXN1L |
342371 |
P0C7T5 |
0.63 |
RRAGC |
64121 |
Q9HB90 |
0.68 |
ATP6V1B2 |
526 |
P21281 |
0.70 |
MTOR |
2475 |
P42345 |
0.74 |
LAMTOR3 |
8649 |
Q9UHA4 |
0.87 |
LAMTOR2 |
28956 |
Q9Y2Q5 |
0.87 |
NOL8 |
55035 |
Q76FK4 |
0.87 |
RRAGB |
10325 |
Q5VZM2 |
0.96 |
RRAGA |
10670 |
Q7L523 |
0.96 |
LGALS3 |
3958 |
P17931 |
0.63 |
LGALS8 |
3964 |
O00214 |
0.63 |
LGALS9 |
3965 |
O00182 |
0.63 |
MPP3 |
4356 |
Q13368 |
0.63 |
TRAF6 |
7189 |
Q9Y4K3 |
0.63 |
TSC2 |
7249 |
P49815 |
0.63 |
SQSTM1 |
8878 |
Q13501 |
0.63 |
MIOS |
54468 |
Q9NXC5 |
0.63 |
WDR24 |
84219 |
Q96S15 |
0.63 |
SLC38A9 |
153129 |
Q8NBW4 |
0.63 |
LGALS9C |
654346 |
Q6DKI2 |
0.63 |
DEPDC5 |
9681 |
O75140 |
0.68 |
RRAGD |
58528 |
Q9NQL2 |
0.70 |
LAMTOR5 |
10542 |
O43504 |
0.82 |
LAMTOR4 |
389541 |
Q0VGL1 |
0.82 |
RPTOR |
57521 |
Q8N122 |
0.86 |
LAMTOR1 |
55004 |
Q6IAA8 |
0.88 |