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Ras-related GTP-binding protein A (Rag A) (RagA) (Adenovirus E3 14.7 kDa-interacting protein 1) (FIP-1)

 RRAGA_HUMAN             Reviewed;         313 AA.
Q7L523; B2R7L1; O00290; Q15347;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
20-DEC-2017, entry version 134.
RecName: Full=Ras-related GTP-binding protein A {ECO:0000305};
Short=Rag A {ECO:0000303|PubMed:11073942};
Short=RagA {ECO:0000303|PubMed:7499430};
AltName: Full=Adenovirus E3 14.7 kDa-interacting protein 1 {ECO:0000303|PubMed:8995684};
AltName: Full=FIP-1 {ECO:0000303|PubMed:8995684};
Name=RRAGA {ECO:0000312|HGNC:HGNC:16963};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000312|EMBL:CAA62131.1}
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain {ECO:0000312|EMBL:CAA62131.1};
PubMed=7499430; DOI=10.1074/jbc.270.48.28982;
Schuermann A., Brauers A., Massmann S., Becker W., Joost H.-G.;
"Cloning of a novel family of mammalian GTP-binding proteins (RagA,
RagBs, RagBl) with remote similarity to the Ras-related GTPases.";
J. Biol. Chem. 270:28982-28988(1995).
[2] {ECO:0000305, ECO:0000312|EMBL:AAB63255.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ADENOVIRUS E3
14.7 KDA PROTEIN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8995684;
Li Y., Kang J., Horwitz M.S.;
"Interaction of an adenovirus 14.7-kilodalton protein inhibitor of
tumor necrosis factor alpha cytolysis with a new member of the GTPase
superfamily of signal transducers.";
J. Virol. 71:1576-1582(1997).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9394008;
Hirose E., Nakashima N., Sekiguchi T., Nishimoto T.;
"RagA is a functional homologue of S. cerevisiae Gtr1p involved in the
Ran/Gsp1-GTPase pathway.";
J. Cell Sci. 111:11-21(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5] {ECO:0000312|EMBL:CAH72136.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000312|EMBL:AAH06433.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:AAH09990.1}, and
Ovary {ECO:0000312|EMBL:AAH06433.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8] {ECO:0000305}
INTERACTION WITH RRAGC AND RRAGD.
PubMed=11073942; DOI=10.1074/jbc.M004389200;
Sekiguchi T., Hirose E., Nakashima N., Ii M., Nishimoto T.;
"Novel G proteins, Rag C and Rag D, interact with GTP-binding
proteins, Rag A and Rag B.";
J. Biol. Chem. 276:7246-7257(2001).
[9] {ECO:0000305}
INTERACTION WITH NOL8, SUBUNIT, AND GTP-BINDING.
PubMed=14660641; DOI=10.1074/jbc.M305935200;
Sekiguchi T., Todaka Y., Wang Y., Hirose E., Nakashima N.,
Nishimoto T.;
"A novel human nucleolar protein, Nop132, binds to the G proteins,
RRAG A/C/D.";
J. Biol. Chem. 279:8343-8350(2004).
[10]
INTERACTION WITH RPTOR.
PubMed=18497260; DOI=10.1126/science.1157535;
Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C.,
Bar-Peled L., Sabatini D.M.;
"The Rag GTPases bind raptor and mediate amino acid signaling to
mTORC1.";
Science 320:1496-1501(2008).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RRAGC.
PubMed=20381137; DOI=10.1016/j.cell.2010.02.024;
Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S.,
Sabatini D.M.;
"Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is
necessary for its activation by amino acids.";
Cell 141:290-303(2010).
[12]
INTERACTION WITH SH3BP4.
PubMed=22575674; DOI=10.1016/j.molcel.2012.04.007;
Kim Y.M., Stone M., Hwang T.H., Kim Y.G., Dunlevy J.R., Griffin T.J.,
Kim D.H.;
"SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1
signaling.";
Mol. Cell 46:833-846(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
ENZYME REGULATION, AND INTERACTION WITH THE GATOR1 COMPLEX.
PubMed=23723238; DOI=10.1126/science.1232044;
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W.,
Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M.,
Sabatini D.M.;
"A Tumor suppressor complex with GAP activity for the Rag GTPases that
signal amino acid sufficiency to mTORC1.";
Science 340:1100-1106(2013).
[15]
INTERACTION WITH SESN1; SESN2 AND SESN3.
PubMed=25259925; DOI=10.1016/j.cell.2014.08.038;
Peng M., Yin N., Li M.O.;
"Sestrins function as guanine nucleotide dissociation inhibitors for
Rag GTPases to control mTORC1 signaling.";
Cell 159:122-133(2014).
[16]
INTERACTION WITH SLC38A9.
PubMed=25561175; DOI=10.1038/nature14107;
Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M.,
Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L.,
Bruckner M., Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W.,
Heinz L.X., Kraft C., Bennett K.L., Indiveri C., Huber L.A.,
Superti-Furga G.;
"SLC38A9 is a component of the lysosomal amino acid sensing machinery
that controls mTORC1.";
Nature 519:477-481(2015).
[17]
INTERACTION WITH SLC38A9.
PubMed=25567906; DOI=10.1126/science.1257132;
Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E.,
Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T.,
Bar-Peled L., Zoncu R., Straub C., Kim C., Park J., Sabatini B.L.,
Sabatini D.M.;
"Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine
sufficiency to mTORC1.";
Science 347:188-194(2015).
[18]
FUNCTION, ENZYME REGULATION, UBIQUITINATION AT LYS-142; LYS-220;
LYS-230 AND LYS-244 BY RNF152, INTERACTION WITH RNF152; TSC2 AND THE
GATOR1 COMPLEX, AND MUTAGENESIS OF LYS-142; LYS-220; LYS-230 AND
LYS-244.
PubMed=25936802; DOI=10.1016/j.molcel.2015.03.033;
Deng L., Jiang C., Chen L., Jin J., Wei J., Zhao L., Chen M., Pan W.,
Xu Y., Chu H., Wang X., Ge X., Li D., Liao L., Liu M., Li L., Wang P.;
"The ubiquitination of RagA GTPase by RNF152 negatively regulates
mTORC1 activation.";
Mol. Cell 58:804-818(2015).
-!- FUNCTION: Guanine nucleotide-binding protein that plays a crucial
role in the cellular response to amino acid availability through
regulation of the mTORC1 signaling cascade. Forms heterodimeric
Rag complexes with RRAGC or RRAGD and cycles between an inactive
GDP-bound and an active GTP-bound form. In its active form
participates in the relocalization of mTORC1 to the lysosomes and
its subsequent activation by the GTPase RHEB. Involved in the
RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha
signaling pathway leading to induction of cell death. May
alternatively act as a cellular target for adenovirus E3-14.7K, an
inhibitor of TNF-alpha functions, thereby affecting cell death.
{ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:25936802,
ECO:0000269|PubMed:8995684, ECO:0000269|PubMed:9394008}.
-!- ENZYME REGULATION: The activation of GTP-binding proteins is
generally mediated by a guanine exchange factor (GEF), while
inactivation through hydrolysis of bound GTP is catalyzed by a
GTPase activating protein (GAP) (PubMed:25936802). The GATOR1
complex functions as a GAP and stimulates RRAGA GTPase activity to
turn it into its inactive GDP-bound form (PubMed:25936802,
PubMed:23723238). {ECO:0000269|PubMed:23723238,
ECO:0000303|PubMed:25936802}.
-!- SUBUNIT: Can occur as a homodimer or as a heterodimer with RRAGC
or RRAGD in a sequence-independent manner; heterodimerization
stabilizes proteins of the heterodimer (PubMed:11073942,
PubMed:20381137). In complex with RRAGC, but not with RRAGB,
interacts with RPTOR (PubMed:18497260). The GTP-bound form of
RRAGA interacts with NOL8 (PubMed:14660641). Interacts with
SH3BP4; the interaction with this negative regulator is most
probably direct, preferentially occurs with the inactive GDP-bound
form of RRAGA and is negatively regulated by amino acids
(PubMed:22575674). The Rag heterodimer interacts with SLC38A9; the
probable amino acid sensor (PubMed:25561175, PubMed:25567906).
Interacts (inactive GDP-bound form) with RNF152; stimulated by
amino acid starvation (PubMed:25936802). Interacts
(polyubiquitinated) with the GATOR1 complex; inactivates RRAGA
(PubMed:25936802). Interacts (polyubiquitinated) with TSC2
(PubMed:25936802). Interacts with adenovirus E3 14.7 kDa protein
(PubMed:8995684). Interacts with SESN1, SESN2 AND SESN3
(PubMed:25259925). {ECO:0000269|PubMed:11073942,
ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:18497260,
ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22575674,
ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25259925,
ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906,
ECO:0000269|PubMed:25936802, ECO:0000269|PubMed:8995684}.
-!- INTERACTION:
Q6IAA8:LAMTOR1; NbExp=11; IntAct=EBI-752376, EBI-715385;
Q9HB90:RRAGC; NbExp=19; IntAct=EBI-752376, EBI-752390;
Q9NQL2:RRAGD; NbExp=8; IntAct=EBI-752376, EBI-992949;
Q8NBW4:SLC38A9; NbExp=12; IntAct=EBI-752376, EBI-9978316;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8995684,
ECO:0000269|PubMed:9394008}. Nucleus {ECO:0000269|PubMed:8995684,
ECO:0000269|PubMed:9394008}. Lysosome
{ECO:0000269|PubMed:20381137}. Note=Predominantly cytoplasmic. May
shuttle between the cytoplasm and nucleus, depending on the bound
nucleotide state (PubMed:8995684, PubMed:9394008). Colocalizes in
vivo with adenovirus E3-14.7K mainly to the cytoplasm especially
near the nuclear membrane and in discrete foci on or near the
plasma membrane (PubMed:8995684). {ECO:0000269|PubMed:20381137,
ECO:0000269|PubMed:8995684, ECO:0000269|PubMed:9394008}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels of
expression in skeletal muscle, heart, and brain.
{ECO:0000269|PubMed:8995684}.
-!- PTM: Ubiquitinated. 'Lys-68'-linked polyubiquitination of the GDP-
bound inactive form of RRAGA by RNF152 is increased in response to
amino acid starvation. Polyubiquitination promotes interaction
with the GATOR1 complex. This does not affect RRAGA degradation.
{ECO:0000269|PubMed:25936802}.
-!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
{ECO:0000305}.
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EMBL; X90529; CAA62131.1; -; mRNA.
EMBL; U41654; AAB63255.1; -; mRNA.
EMBL; AL356000; CAH72136.1; -; Genomic_DNA.
EMBL; AK313023; BAG35858.1; -; mRNA.
EMBL; CH471071; EAW58653.1; -; Genomic_DNA.
EMBL; BC006433; AAH06433.1; -; mRNA.
EMBL; BC009990; AAH09990.1; -; mRNA.
CCDS; CCDS6488.1; -.
PIR; I38176; I38176.
RefSeq; NP_006561.1; NM_006570.4.
UniGene; Hs.743260; -.
PDB; 6EHR; X-ray; 2.90 A; F=183-313.
PDBsum; 6EHR; -.
ProteinModelPortal; Q7L523; -.
SMR; Q7L523; -.
BioGrid; 115912; 21.
DIP; DIP-37516N; -.
IntAct; Q7L523; 12.
MINT; MINT-155844; -.
STRING; 9606.ENSP00000369899; -.
iPTMnet; Q7L523; -.
PhosphoSitePlus; Q7L523; -.
BioMuta; RRAGA; -.
DMDM; 74759007; -.
EPD; Q7L523; -.
MaxQB; Q7L523; -.
PaxDb; Q7L523; -.
PeptideAtlas; Q7L523; -.
PRIDE; Q7L523; -.
DNASU; 10670; -.
Ensembl; ENST00000380527; ENSP00000369899; ENSG00000155876.
GeneID; 10670; -.
KEGG; hsa:10670; -.
UCSC; uc003znj.4; human.
CTD; 10670; -.
DisGeNET; 10670; -.
EuPathDB; HostDB:ENSG00000155876.5; -.
GeneCards; RRAGA; -.
HGNC; HGNC:16963; RRAGA.
HPA; HPA003734; -.
MIM; 612194; gene.
neXtProt; NX_Q7L523; -.
OpenTargets; ENSG00000155876; -.
PharmGKB; PA134980509; -.
eggNOG; KOG3886; Eukaryota.
eggNOG; ENOG410XQ0R; LUCA.
GeneTree; ENSGT00550000074769; -.
HOGENOM; HOG000173258; -.
HOVERGEN; HBG052715; -.
InParanoid; Q7L523; -.
KO; K16185; -.
OMA; SRPLECV; -.
OrthoDB; EOG091G050Q; -.
PhylomeDB; Q7L523; -.
TreeFam; TF300616; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-165159; mTOR signalling.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SIGNOR; Q7L523; -.
ChiTaRS; RRAGA; human.
GeneWiki; RRAGA; -.
GenomeRNAi; 10670; -.
PRO; PR:Q7L523; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000155876; -.
CleanEx; HS_RRAGA; -.
Genevisible; Q7L523; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0034448; C:EGO complex; IBA:GO_Central.
GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IBA:GO_Central.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:SGD.
GO; GO:0051219; F:phosphoprotein binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0008219; P:cell death; IDA:UniProtKB.
GO; GO:0034613; P:cellular protein localization; IMP:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; IDA:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
GO; GO:0045919; P:positive regulation of cytolysis; IDA:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; NAS:UniProtKB.
GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
InterPro; IPR006762; Gtr1_RagA.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11259; PTHR11259; 2.
Pfam; PF04670; Gtr1_RagA; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Cytoplasm; GTP-binding;
Host-virus interaction; Isopeptide bond; Lysosome; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 313 Ras-related GTP-binding protein A.
/FTId=PRO_0000239945.
NP_BIND 14 21 GTP. {ECO:0000250|UniProtKB:Q00582}.
NP_BIND 62 66 GTP. {ECO:0000250|UniProtKB:Q00582}.
NP_BIND 127 130 GTP. {ECO:0000250|UniProtKB:Q00582}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25936802}.
CROSSLNK 220 220 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25936802}.
CROSSLNK 230 230 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25936802}.
CROSSLNK 244 244 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25936802}.
MUTAGEN 142 142 K->R: Prevents RRAGA ubiquitination and
alters interaction and regulation by
GATOR1; when associated with R-220, R-230
and R-244. {ECO:0000269|PubMed:25936802}.
MUTAGEN 220 220 K->R: Prevents RRAGA ubiquitination and
alters interaction and regulation by
GATOR1; when associated with R-142, R-230
and R-244. {ECO:0000269|PubMed:25936802}.
MUTAGEN 230 230 K->R: Prevents RRAGA ubiquitination and
alters interaction and regulation by
GATOR1; when associated with RR-142, R-
220 and R-244.
{ECO:0000269|PubMed:25936802}.
MUTAGEN 244 244 K->R: Prevents RRAGA ubiquitination and
alters interaction and regulation by
GATOR1; when associated with RR-142, R-
220 and R-230.
{ECO:0000269|PubMed:25936802}.
CONFLICT 229 229 E -> G (in Ref. 2; AAB63255).
{ECO:0000305}.
CONFLICT 246 246 A -> P (in Ref. 2; AAB63255).
{ECO:0000305}.
HELIX 183 197 {ECO:0000244|PDB:6EHR}.
STRAND 201 207 {ECO:0000244|PDB:6EHR}.
TURN 208 210 {ECO:0000244|PDB:6EHR}.
STRAND 213 218 {ECO:0000244|PDB:6EHR}.
HELIX 230 244 {ECO:0000244|PDB:6EHR}.
STRAND 249 255 {ECO:0000244|PDB:6EHR}.
STRAND 260 265 {ECO:0000244|PDB:6EHR}.
STRAND 267 277 {ECO:0000244|PDB:6EHR}.
HELIX 283 297 {ECO:0000244|PDB:6EHR}.
SEQUENCE 313 AA; 36566 MW; B0DA1FC8FA6B766A CRC64;
MPNTAMKKKV LLMGKSGSGK TSMRSIIFAN YIARDTRRLG ATIDVEHSHV RFLGNLVLNL
WDCGGQDTFM ENYFTSQRDN IFRNVEVLIY VFDVESRELE KDMHYYQSCL EAILQNSPDA
KIFCLVHKMD LVQEDQRDLI FKEREEDLRR LSRPLECACF RTSIWDETLY KAWSSIVYQL
IPNVQQLEMN LRNFAQIIEA DEVLLFERAT FLVISHYQCK EQRDVHRFEK ISNIIKQFKL
SCSKLAASFQ SMEVRNSNFA AFIDIFTSNT YVMVVMSDPS IPSAATLINI RNARKHFEKL
ERVDGPKHSL LMR


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