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Protein

Ras-related GTP-binding protein B

Gene

RRAGB

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.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). The GATOR1 complex functions as a GAP and stimulates RRAGB GTPase activity to turn it into its inactive GDP-bound form.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi47 – 548GTPBy similarity
Nucleotide bindingi123 – 1275GTPBy similarity
Nucleotide bindingi188 – 1914GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB
  • guanyl ribonucleotide binding Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: Reactome
  • cellular protein localization Source: UniProtKB
  • cellular response to amino acid starvation Source: UniProtKB
  • cellular response to amino acid stimulus Source: UniProtKB
  • macroautophagy Source: Reactome
  • positive regulation of TOR signaling Source: UniProtKB
  • regulation of autophagy Source: GO_Central
  • regulation of TOR signaling Source: UniProtKB
Complete GO annotation...

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 BCurated
Short name:
Rag B1 Publication
Short name:
RagB1 Publication
Gene namesi
Name:RRAGBImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:19901. RRAGB.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Lysosome 1 Publication

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • 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: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541T → L: Decreased RPTOR-binding. 1 Publication
Mutagenesisi127 – 1271Q → L: Increased RPTOR-binding. 1 Publication

Organism-specific databases

PharmGKBiPA134902397.

Polymorphism and mutation databases

BioMutaiRRAGB.
DMDMi74747821.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Ras-related GTP-binding protein BPRO_0000239948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ5VZM2.
MaxQBiQ5VZM2.
PaxDbiQ5VZM2.
PRIDEiQ5VZM2.

PTM databases

iPTMnetiQ5VZM2.
PhosphoSiteiQ5VZM2.

Expressioni

Gene expression databases

BgeeiQ5VZM2.
CleanExiHS_RRAGB.
ExpressionAtlasiQ5VZM2. baseline and differential.
GenevisibleiQ5VZM2. HS.

Organism-specific databases

HPAiHPA003734.

Interactioni

Subunit structurei

Interacts with RRAGC and RRAGD; heterodimerization stabilizes RRAG proteins (PubMed:11073942). In complex with RRAGC, but not with RRAGA, interacts with RPTOR; this interaction is particularly efficient with GTP-loaded RRAGB and GDP-loaded RRAGC (PubMed:18497260). Interacts with SH3BP4; the interaction with this negative regulator is most probably direct, preferentially occurs with the inactive GDP-bound form of RRAGB, is negatively regulated by amino acids and prevents interaction with RPTOR (PubMed:22575674). Interacts with the GATOR1 complex; inactivates RRAGB (PubMed:23723238). The Rag heterodimer interacts with SLC38A9; the probable amino acid sensor (PubMed:25561175, PubMed:25567906).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LAMP1P112792EBI-993049,EBI-2805407
RRAGCQ9HB905EBI-993049,EBI-752390
RRAGDQ9NQL27EBI-993049,EBI-992949

Protein-protein interaction databases

BioGridi115608. 31 interactions.
DIPiDIP-37518N.
IntActiQ5VZM2. 13 interactions.
STRINGi9606.ENSP00000262850.

Structurei

3D structure databases

ProteinModelPortaliQ5VZM2.
SMRiQ5VZM2. Positions 39-358.
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.
InParanoidiQ5VZM2.
KOiK16185.
OMAiDIAAKPR.
OrthoDBiEOG7XM2Z4.
PhylomeDBiQ5VZM2.
TreeFamiTF300616.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11259. PTHR11259. 2 hits.
PfamiPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q5VZM2-1) [UniParc]FASTAAdd to basket

Also known as: Long1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEESDSEKTT EKENLGPRMD PPLGEPEGSL GWVLPNTAMK KKVLLMGKSG
60 70 80 90 100
SGKTSMRSII FANYIARDTR RLGATILDRI HSLQINSSLS TYSLVDSVGN
110 120 130 140 150
TKTFDVEHSH VRFLGNLVLN LWDCGGQDTF MENYFTSQRD NIFRNVEVLI
160 170 180 190 200
YVFDVESREL EKDMHYYQSC LEAILQNSPD AKIFCLVHKM DLVQEDQRDL
210 220 230 240 250
IFKEREEDLR RLSRPLECSC FRTSIWDETL YKAWSSIVYQ LIPNVQQLEM
260 270 280 290 300
NLRNFAEIIE ADEVLLFERA TFLVISHYQC KEQRDAHRFE KISNIIKQFK
310 320 330 340 350
LSCSKLAASF QSMEVRNSNF AAFIDIFTSN TYVMVVMSDP SIPSAATLIN
360 370
IRNARKHFEK LERVDGPKQC LLMR
Length:374
Mass (Da):43,250
Last modified:December 7, 2004 - v1
Checksum:i0D32F7D86E2A00DE
GO
Isoform 22 Publications (identifier: Q5VZM2-2) [UniParc]FASTAAdd to basket

Also known as: Short1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     77-104: Missing.

Show »
Length:346
Mass (Da):40,172
Checksum:iF8392F84D72E527C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti337 – 3371M → V in CAA62132 (PubMed:7499430).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei77 – 10428Missing in isoform 2. 5 PublicationsVSP_052073Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90530 mRNA. Translation: CAA62132.1.
AK289407 mRNA. Translation: BAF82096.1.
AL831926 mRNA. Translation: CAD38586.1.
AL139277, AL159987 Genomic DNA. Translation: CAI40804.1.
AL139277, AL159987 Genomic DNA. Translation: CAI40805.1.
AL159987, AL139277 Genomic DNA. Translation: CAH70826.1.
AL159987, AL139277 Genomic DNA. Translation: CAH70827.1.
CH471154 Genomic DNA. Translation: EAW93229.1.
BC034726 mRNA. Translation: AAH34726.1.
CCDSiCCDS14371.1. [Q5VZM2-2]
CCDS14372.1. [Q5VZM2-1]
PIRiI38177.
RefSeqiNP_006055.3. NM_006064.4. [Q5VZM2-2]
NP_057740.2. NM_016656.3. [Q5VZM2-1]
UniGeneiHs.50282.

Genome annotation databases

EnsembliENST00000262850; ENSP00000262850; ENSG00000083750. [Q5VZM2-1]
ENST00000374941; ENSP00000364077; ENSG00000083750. [Q5VZM2-2]
GeneIDi10325.
KEGGihsa:10325.
UCSCiuc004dup.4. human. [Q5VZM2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90530 mRNA. Translation: CAA62132.1.
AK289407 mRNA. Translation: BAF82096.1.
AL831926 mRNA. Translation: CAD38586.1.
AL139277, AL159987 Genomic DNA. Translation: CAI40804.1.
AL139277, AL159987 Genomic DNA. Translation: CAI40805.1.
AL159987, AL139277 Genomic DNA. Translation: CAH70826.1.
AL159987, AL139277 Genomic DNA. Translation: CAH70827.1.
CH471154 Genomic DNA. Translation: EAW93229.1.
BC034726 mRNA. Translation: AAH34726.1.
CCDSiCCDS14371.1. [Q5VZM2-2]
CCDS14372.1. [Q5VZM2-1]
PIRiI38177.
RefSeqiNP_006055.3. NM_006064.4. [Q5VZM2-2]
NP_057740.2. NM_016656.3. [Q5VZM2-1]
UniGeneiHs.50282.

3D structure databases

ProteinModelPortaliQ5VZM2.
SMRiQ5VZM2. Positions 39-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115608. 31 interactions.
DIPiDIP-37518N.
IntActiQ5VZM2. 13 interactions.
STRINGi9606.ENSP00000262850.

PTM databases

iPTMnetiQ5VZM2.
PhosphoSiteiQ5VZM2.

Polymorphism and mutation databases

BioMutaiRRAGB.
DMDMi74747821.

Proteomic databases

EPDiQ5VZM2.
MaxQBiQ5VZM2.
PaxDbiQ5VZM2.
PRIDEiQ5VZM2.

Protocols and materials databases

DNASUi10325.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262850; ENSP00000262850; ENSG00000083750. [Q5VZM2-1]
ENST00000374941; ENSP00000364077; ENSG00000083750. [Q5VZM2-2]
GeneIDi10325.
KEGGihsa:10325.
UCSCiuc004dup.4. human. [Q5VZM2-1]

Organism-specific databases

CTDi10325.
GeneCardsiRRAGB.
HGNCiHGNC:19901. RRAGB.
HPAiHPA003734.
MIMi300725. gene.
neXtProtiNX_Q5VZM2.
PharmGKBiPA134902397.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3886. Eukaryota.
ENOG410XQ0R. LUCA.
GeneTreeiENSGT00550000074769.
HOGENOMiHOG000173258.
HOVERGENiHBG052715.
InParanoidiQ5VZM2.
KOiK16185.
OMAiDIAAKPR.
OrthoDBiEOG7XM2Z4.
PhylomeDBiQ5VZM2.
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

GeneWikiiRRAGB.
GenomeRNAii10325.
PROiQ5VZM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VZM2.
CleanExiHS_RRAGB.
ExpressionAtlasiQ5VZM2. baseline and differential.
GenevisibleiQ5VZM2. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006762. Gtr1_RagA.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11259. PTHR11259. 2 hits.
PfamiPF04670. Gtr1_RagA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
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] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    Tissue: BrainImported.
  2. "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] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
  3. "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] (ISOFORM 2).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Adipose tissue.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [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] (ISOFORM 2).
    Tissue: SkinImported.
  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. "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: FUNCTION, INTERACTION WITH RPTOR, MUTAGENESIS OF THR-54 AND GLN-127.
  10. "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.
  11. "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.
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: FUNCTION, ENZYME REGULATION, INTERACTION WITH THE GATOR1 COMPLEX.
  14. Cited for: SUBUNIT.
  15. Cited for: SUBUNIT.

Entry informationi

Entry nameiRRAGB_HUMAN
AccessioniPrimary (citable) accession number: Q5VZM2
Secondary accession number(s): A8K042, Q15348, Q8N3T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: December 7, 2004
Last modified: June 8, 2016
This is version 103 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 X
    Human chromosome X: 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.