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Protein

Ras-related GTP-binding protein A

Gene

RRAGA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 to 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.4 Publications

Enzyme regulationi

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).1 Publication1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi62 – 665GTPBy similarity
Nucleotide bindingi127 – 1304GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB
  • phosphoprotein binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell cycle arrest Source: Reactome
  • cell death Source: UniProtKB
  • cellular protein localization Source: UniProtKB
  • cellular response to amino acid starvation Source: UniProtKB
  • cellular response to amino acid stimulus Source: UniProtKB
  • macroautophagy Source: Reactome
  • modulation by virus of host morphology or physiology Source: UniProtKB
  • negative regulation of autophagy Source: UniProtKB
  • positive regulation of cytolysis Source: UniProtKB
  • positive regulation of TORC1 signaling Source: UniProtKB
  • positive regulation of TOR signaling Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Host-virus interaction

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1632852. Macroautophagy.
R-HSA-165159. mTOR signalling.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related GTP-binding protein ACurated
Short name:
Rag A1 Publication
Short name:
RagA1 Publication
Alternative name(s):
Adenovirus E3 14.7 kDa-interacting protein 11 Publication
FIP-11 Publication
Gene namesi
Name:RRAGAImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:16963. RRAGA.

Subcellular locationi

  • Cytoplasm 2 Publications
  • Nucleus 2 Publications
  • Lysosome 1 Publication

  • 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).3 Publications

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • EGO complex Source: GO_Central
  • Golgi apparatus Source: HPA
  • Gtr1-Gtr2 GTPase complex Source: GO_Central
  • intracellular membrane-bounded organelle Source: HPA
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi142 – 1421K → R: Prevents RRAGA ubiquitination and alters interaction and regulation by GATOR1; when associated with R-220, R-230 and R-244. 1 Publication
Mutagenesisi220 – 2201K → R: Prevents RRAGA ubiquitination and alters interaction and regulation by GATOR1; when associated with R-142, R-230 and R-244. 1 Publication
Mutagenesisi230 – 2301K → R: Prevents RRAGA ubiquitination and alters interaction and regulation by GATOR1; when associated with RR-142, R-220 and R-244. 1 Publication
Mutagenesisi244 – 2441K → R: Prevents RRAGA ubiquitination and alters interaction and regulation by GATOR1; when associated with RR-142, R-220 and R-230. 1 Publication

Organism-specific databases

PharmGKBiPA134980509.

Polymorphism and mutation databases

BioMutaiRRAGA.
DMDMi74759007.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Ras-related GTP-binding protein APRO_0000239945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki142 – 142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki220 – 220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki244 – 244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei309 – 3091PhosphoserineCombined sources

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ7L523.
MaxQBiQ7L523.
PaxDbiQ7L523.
PeptideAtlasiQ7L523.
PRIDEiQ7L523.

PTM databases

iPTMnetiQ7L523.
PhosphoSiteiQ7L523.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels of expression in skeletal muscle, heart, and brain.1 Publication

Gene expression databases

BgeeiQ7L523.
CleanExiHS_RRAGA.
GenevisibleiQ7L523. HS.

Organism-specific databases

HPAiHPA003734.

Interactioni

Subunit structurei

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).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LAMTOR1Q6IAA810EBI-752376,EBI-715385
RRAGCQ9HB9018EBI-752376,EBI-752390
RRAGDQ9NQL28EBI-752376,EBI-992949
SLC38A9Q8NBW411EBI-752376,EBI-9978316

GO - Molecular functioni

  • phosphoprotein binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115912. 20 interactions.
DIPiDIP-37516N.
IntActiQ7L523. 10 interactions.
MINTiMINT-155844.
STRINGi9606.ENSP00000369899.

Structurei

3D structure databases

ProteinModelPortaliQ7L523.
SMRiQ7L523. Positions 7-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTR/RAG GTP-binding protein family.Curated

Phylogenomic databases

eggNOGiKOG3886. Eukaryota.
ENOG410XQ0R. LUCA.
GeneTreeiENSGT00550000074769.
HOGENOMiHOG000173258.
HOVERGENiHBG052715.
InParanoidiQ7L523.
KOiK16185.
OMAiISHCQRK.
OrthoDBiEOG7XM2Z4.
PhylomeDBiQ7L523.
TreeFamiTF300616.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11259. PTHR11259. 1 hit.
PfamiPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7L523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNTAMKKKV LLMGKSGSGK TSMRSIIFAN YIARDTRRLG ATIDVEHSHV
60 70 80 90 100
RFLGNLVLNL WDCGGQDTFM ENYFTSQRDN IFRNVEVLIY VFDVESRELE
110 120 130 140 150
KDMHYYQSCL EAILQNSPDA KIFCLVHKMD LVQEDQRDLI FKEREEDLRR
160 170 180 190 200
LSRPLECACF RTSIWDETLY KAWSSIVYQL IPNVQQLEMN LRNFAQIIEA
210 220 230 240 250
DEVLLFERAT FLVISHYQCK EQRDVHRFEK ISNIIKQFKL SCSKLAASFQ
260 270 280 290 300
SMEVRNSNFA AFIDIFTSNT YVMVVMSDPS IPSAATLINI RNARKHFEKL
310
ERVDGPKHSL LMR
Length:313
Mass (Da):36,566
Last modified:July 5, 2004 - v1
Checksum:iB0DA1FC8FA6B766A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291E → G in AAB63255 (PubMed:8995684).Curated
Sequence conflicti246 – 2461A → P in AAB63255 (PubMed:8995684).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90529 mRNA. Translation: CAA62131.1.
U41654 mRNA. Translation: AAB63255.1.
AL356000 Genomic DNA. Translation: CAH72136.1.
AK313023 mRNA. Translation: BAG35858.1.
CH471071 Genomic DNA. Translation: EAW58653.1.
BC006433 mRNA. Translation: AAH06433.1.
BC009990 mRNA. Translation: AAH09990.1.
CCDSiCCDS6488.1.
PIRiI38176.
RefSeqiNP_006561.1. NM_006570.4.
UniGeneiHs.743260.

Genome annotation databases

EnsembliENST00000380527; ENSP00000369899; ENSG00000155876.
GeneIDi10670.
KEGGihsa:10670.
UCSCiuc003znj.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90529 mRNA. Translation: CAA62131.1.
U41654 mRNA. Translation: AAB63255.1.
AL356000 Genomic DNA. Translation: CAH72136.1.
AK313023 mRNA. Translation: BAG35858.1.
CH471071 Genomic DNA. Translation: EAW58653.1.
BC006433 mRNA. Translation: AAH06433.1.
BC009990 mRNA. Translation: AAH09990.1.
CCDSiCCDS6488.1.
PIRiI38176.
RefSeqiNP_006561.1. NM_006570.4.
UniGeneiHs.743260.

3D structure databases

ProteinModelPortaliQ7L523.
SMRiQ7L523. Positions 7-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115912. 20 interactions.
DIPiDIP-37516N.
IntActiQ7L523. 10 interactions.
MINTiMINT-155844.
STRINGi9606.ENSP00000369899.

PTM databases

iPTMnetiQ7L523.
PhosphoSiteiQ7L523.

Polymorphism and mutation databases

BioMutaiRRAGA.
DMDMi74759007.

Proteomic databases

EPDiQ7L523.
MaxQBiQ7L523.
PaxDbiQ7L523.
PeptideAtlasiQ7L523.
PRIDEiQ7L523.

Protocols and materials databases

DNASUi10670.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380527; ENSP00000369899; ENSG00000155876.
GeneIDi10670.
KEGGihsa:10670.
UCSCiuc003znj.4. human.

Organism-specific databases

CTDi10670.
GeneCardsiRRAGA.
HGNCiHGNC:16963. RRAGA.
HPAiHPA003734.
MIMi612194. gene.
neXtProtiNX_Q7L523.
PharmGKBiPA134980509.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3886. Eukaryota.
ENOG410XQ0R. LUCA.
GeneTreeiENSGT00550000074769.
HOGENOMiHOG000173258.
HOVERGENiHBG052715.
InParanoidiQ7L523.
KOiK16185.
OMAiISHCQRK.
OrthoDBiEOG7XM2Z4.
PhylomeDBiQ7L523.
TreeFamiTF300616.

Enzyme and pathway databases

ReactomeiR-HSA-1632852. Macroautophagy.
R-HSA-165159. mTOR signalling.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiRRAGA. human.
GeneWikiiRRAGA.
GenomeRNAii10670.
PROiQ7L523.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L523.
CleanExiHS_RRAGA.
GenevisibleiQ7L523. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11259. PTHR11259. 1 hit.
PfamiPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagBl) with remote similarity to the Ras-related GTPases."
    Schuermann A., Brauers A., Massmann S., Becker W., Joost H.-G.
    J. Biol. Chem. 270:28982-28988(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brainImported.
  2. "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."
    Li Y., Kang J., Horwitz M.S.
    J. Virol. 71:1576-1582(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ADENOVIRUS E3 14.7 KDA PROTEIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway."
    Hirose E., Nakashima N., Sekiguchi T., Nishimoto T.
    J. Cell Sci. 111:11-21(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.
  5. "DNA sequence and analysis of human chromosome 9."
    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.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported and OvaryImported.
  8. "Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B."
    Sekiguchi T., Hirose E., Nakashima N., Ii M., Nishimoto T.
    J. Biol. Chem. 276:7246-7257(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RRAGC AND RRAGD.
  9. "A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D."
    Sekiguchi T., Todaka Y., Wang Y., Hirose E., Nakashima N., Nishimoto T.
    J. Biol. Chem. 279:8343-8350(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOL8, SUBUNIT, GTP-BINDING.
  10. "The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1."
    Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C., Bar-Peled L., Sabatini D.M.
    Science 320:1496-1501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPTOR.
  11. "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids."
    Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.
    Cell 141:290-303(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAGC.
  12. "SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1 signaling."
    Kim Y.M., Stone M., Hwang T.H., Kim Y.G., Dunlevy J.R., Griffin T.J., Kim D.H.
    Mol. Cell 46:833-846(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH3BP4.
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  14. "A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1."
    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.
    Science 340:1100-1106(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH THE GATOR1 COMPLEX.
  15. "Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling."
    Peng M., Yin N., Li M.O.
    Cell 159:122-133(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SESN1; SESN2 AND SESN3.
  16. Cited for: INTERACTION WITH SLC38A9.
  17. Cited for: INTERACTION WITH SLC38A9.
  18. "The ubiquitination of RagA GTPase by RNF152 negatively regulates mTORC1 activation."
    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.
    Mol. Cell 58:804-818(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, UBIQUITINATION AT LYS-142; LYS-220; LYS-230 AND LYS-244 BY RNF152, INTERACTION WITH RNF152; TSC2 AND THE GATOR1 COMPLEX, MUTAGENESIS OF LYS-142; LYS-220; LYS-230 AND LYS-244.

Entry informationi

Entry nameiRRAGA_HUMAN
AccessioniPrimary (citable) accession number: Q7L523
Secondary accession number(s): B2R7L1, O00290, Q15347
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.