RRAGB_HUMAN
ID RRAGB_HUMAN Reviewed; 374 AA.
AC Q5VZM2; A8K042; Q15348; Q8N3T0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ras-related GTP-binding protein B {ECO:0000305};
DE Short=Rag B {ECO:0000303|PubMed:11073942};
DE Short=RagB {ECO:0000303|PubMed:7499430};
DE EC=3.6.5.- {ECO:0000269|PubMed:23723238, ECO:0000305|PubMed:24095279};
GN Name=RRAGB {ECO:0000312|HGNC:HGNC:19901};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA62132.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Brain {ECO:0000312|EMBL:CAA62132.1};
RX PubMed=7499430; DOI=10.1074/jbc.270.48.28982;
RA Schuermann A., Brauers A., Massmann S., Becker W., Joost H.-G.;
RT "Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs,
RT RagBl) with remote similarity to the Ras-related GTPases.";
RL J. Biol. Chem. 270:28982-28988(1995).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9394008; DOI=10.1242/jcs.111.1.11;
RA Hirose E., Nakashima N., Sekiguchi T., Nishimoto T.;
RT "RagA is a functional homologue of S. cerevisiae Gtr1p involved in the
RT Ran/Gsp1-GTPase pathway.";
RL J. Cell Sci. 111:11-21(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adipose tissue;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5] {ECO:0000312|EMBL:AL159987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6] {ECO:0000305, ECO:0000312|EMBL:CAD38586.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAH34726.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin {ECO:0000312|EMBL:AAH34726.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8] {ECO:0000305}
RP INTERACTION WITH RRAGC AND RRAGD.
RX PubMed=11073942; DOI=10.1074/jbc.m004389200;
RA Sekiguchi T., Hirose E., Nakashima N., Ii M., Nishimoto T.;
RT "Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag
RT A and Rag B.";
RL J. Biol. Chem. 276:7246-7257(2001).
RN [9]
RP FUNCTION, INTERACTION WITH RPTOR, AND MUTAGENESIS OF THR-54 AND GLN-127.
RX PubMed=18497260; DOI=10.1126/science.1157535;
RA Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C.,
RA Bar-Peled L., Sabatini D.M.;
RT "The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1.";
RL Science 320:1496-1501(2008).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20381137; DOI=10.1016/j.cell.2010.02.024;
RA Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.;
RT "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is
RT necessary for its activation by amino acids.";
RL Cell 141:290-303(2010).
RN [11]
RP INTERACTION WITH SH3BP4.
RX PubMed=22575674; DOI=10.1016/j.molcel.2012.04.007;
RA Kim Y.M., Stone M., Hwang T.H., Kim Y.G., Dunlevy J.R., Griffin T.J.,
RA Kim D.H.;
RT "SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1
RT signaling.";
RL Mol. Cell 46:833-846(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-54 AND GLN-127.
RX PubMed=24095279; DOI=10.1016/j.molcel.2013.09.016;
RA Tsun Z.Y., Bar-Peled L., Chantranupong L., Zoncu R., Wang T., Kim C.,
RA Spooner E., Sabatini D.M.;
RT "The folliculin tumor suppressor is a GAP for the RagC/D GTPases that
RT signal amino acid levels to mTORC1.";
RL Mol. Cell 52:495-505(2013).
RN [15]
RP INTERACTION WITH SESN1; SESN2 AND SESN3.
RX PubMed=25259925; DOI=10.1016/j.cell.2014.08.038;
RA Peng M., Yin N., Li M.O.;
RT "Sestrins function as guanine nucleotide dissociation inhibitors for Rag
RT GTPases to control mTORC1 signaling.";
RL Cell 159:122-133(2014).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH THE
RP GATOR1 COMPLEX.
RX PubMed=23723238; DOI=10.1126/science.1232044;
RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A.,
RA Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.;
RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that
RT signal amino acid sufficiency to mTORC1.";
RL Science 340:1100-1106(2013).
RN [17]
RP SUBUNIT.
RX PubMed=25561175; DOI=10.1038/nature14107;
RA Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M.,
RA Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L., Bruckner M.,
RA Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W., Heinz L.X.,
RA Kraft C., Bennett K.L., Indiveri C., Huber L.A., Superti-Furga G.;
RT "SLC38A9 is a component of the lysosomal amino acid sensing machinery that
RT controls mTORC1.";
RL Nature 519:477-481(2015).
RN [18]
RP SUBUNIT.
RX PubMed=25567906; DOI=10.1126/science.1257132;
RA Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E.,
RA Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T., Bar-Peled L.,
RA Zoncu R., Straub C., Kim C., Park J., Sabatini B.L., Sabatini D.M.;
RT "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine
RT sufficiency to mTORC1.";
RL Science 347:188-194(2015).
CC -!- FUNCTION: Guanine nucleotide-binding protein that plays a crucial role
CC in the cellular response to amino acid availability through regulation
CC of the mTORC1 signaling cascade (PubMed:18497260, PubMed:20381137,
CC PubMed:24095279, PubMed:23723238). Forms heterodimeric Rag complexes
CC with RRAGC or RRAGD and cycles between an inactive GDP-bound and an
CC active GTP-bound form (PubMed:18497260, PubMed:20381137,
CC PubMed:24095279, PubMed:23723238). In its active form participates in
CC the relocalization of mTORC1 to the lysosomes and its subsequent
CC activation by the GTPase RHEB (PubMed:18497260, PubMed:20381137,
CC PubMed:23723238). Involved in the RCC1/Ran-GTPase pathway
CC (PubMed:9394008). {ECO:0000269|PubMed:18497260,
CC ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:23723238,
CC ECO:0000269|PubMed:24095279, ECO:0000269|PubMed:9394008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:23723238, ECO:0000305|PubMed:24095279};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:23723238, ECO:0000305|PubMed:24095279};
CC -!- ACTIVITY REGULATION: The activation of GTP-binding proteins is
CC generally mediated by a guanine exchange factor (GEF), while
CC inactivation through hydrolysis of bound GTP is catalyzed by a GTPase
CC activating protein (GAP). The GATOR1 complex functions as a GAP and
CC stimulates RRAGB GTPase activity to turn it into its inactive GDP-bound
CC form. {ECO:0000269|PubMed:23723238}.
CC -!- SUBUNIT: Interacts with RRAGC and RRAGD; heterodimerization stabilizes
CC RRAG proteins (PubMed:11073942). In complex with RRAGC, but not with
CC RRAGA, interacts with RPTOR; this interaction is particularly efficient
CC with GTP-loaded RRAGB and GDP-loaded RRAGC (PubMed:18497260). Component
CC of the lysosomal folliculin complex (LFC), composed of FLCN, FNIP1 (or
CC FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD
CC GTP-bound, and Ragulator (By similarity). Interacts with SH3BP4; the
CC interaction with this negative regulator is most probably direct,
CC preferentially occurs with the inactive GDP-bound form of RRAGB, is
CC negatively regulated by amino acids and prevents interaction with RPTOR
CC (PubMed:22575674). Interacts with the GATOR1 complex; inactivates RRAGB
CC (PubMed:23723238). The Rag heterodimer interacts with SLC38A9; the
CC probable amino acid sensor (PubMed:25561175, PubMed:25567906).
CC Interacts with SESN1, SESN2 and SESN3 (PubMed:25259925).
CC {ECO:0000250|UniProtKB:Q7L523, ECO:0000269|PubMed:11073942,
CC ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:22575674,
CC ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25259925,
CC ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906}.
CC -!- INTERACTION:
CC Q5VZM2; P11279: LAMP1; NbExp=2; IntAct=EBI-993049, EBI-2805407;
CC Q5VZM2; Q9HB90: RRAGC; NbExp=8; IntAct=EBI-993049, EBI-752390;
CC Q5VZM2; Q9NQL2: RRAGD; NbExp=7; IntAct=EBI-993049, EBI-992949;
CC Q5VZM2; Q8NBW4: SLC38A9; NbExp=2; IntAct=EBI-993049, EBI-9978316;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9394008}. Lysosome
CC {ECO:0000269|PubMed:20381137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:7499430}; Synonyms=Long
CC {ECO:0000269|PubMed:7499430};
CC IsoId=Q5VZM2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:7499430, ECO:0000269|PubMed:9394008};
CC Synonyms=Short {ECO:0000269|PubMed:7499430};
CC IsoId=Q5VZM2-2; Sequence=VSP_052073;
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000305}.
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DR EMBL; X90530; CAA62132.1; -; mRNA.
DR EMBL; AK289407; BAF82096.1; -; mRNA.
DR EMBL; AL831926; CAD38586.1; -; mRNA.
DR EMBL; AL139277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL159987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471154; EAW93229.1; -; Genomic_DNA.
DR EMBL; BC034726; AAH34726.1; -; mRNA.
DR CCDS; CCDS14371.1; -. [Q5VZM2-2]
DR CCDS; CCDS14372.1; -. [Q5VZM2-1]
DR PIR; I38177; I38177.
DR RefSeq; NP_006055.3; NM_006064.4. [Q5VZM2-2]
DR RefSeq; NP_057740.2; NM_016656.3. [Q5VZM2-1]
DR AlphaFoldDB; Q5VZM2; -.
DR SMR; Q5VZM2; -.
DR BioGRID; 115608; 56.
DR DIP; DIP-37518N; -.
DR IntAct; Q5VZM2; 26.
DR MINT; Q5VZM2; -.
DR STRING; 9606.ENSP00000262850; -.
DR iPTMnet; Q5VZM2; -.
DR PhosphoSitePlus; Q5VZM2; -.
DR BioMuta; RRAGB; -.
DR DMDM; 74747821; -.
DR EPD; Q5VZM2; -.
DR jPOST; Q5VZM2; -.
DR MassIVE; Q5VZM2; -.
DR MaxQB; Q5VZM2; -.
DR PaxDb; Q5VZM2; -.
DR PeptideAtlas; Q5VZM2; -.
DR PRIDE; Q5VZM2; -.
DR ProteomicsDB; 65712; -. [Q5VZM2-1]
DR ProteomicsDB; 65713; -. [Q5VZM2-2]
DR Antibodypedia; 447; 150 antibodies from 26 providers.
DR DNASU; 10325; -.
DR Ensembl; ENST00000262850.7; ENSP00000262850.7; ENSG00000083750.13. [Q5VZM2-1]
DR Ensembl; ENST00000374941.9; ENSP00000364077.4; ENSG00000083750.13. [Q5VZM2-2]
DR GeneID; 10325; -.
DR KEGG; hsa:10325; -.
DR MANE-Select; ENST00000374941.9; ENSP00000364077.4; NM_006064.5; NP_006055.3. [Q5VZM2-2]
DR UCSC; uc004dup.4; human. [Q5VZM2-1]
DR CTD; 10325; -.
DR GeneCards; RRAGB; -.
DR HGNC; HGNC:19901; RRAGB.
DR HPA; ENSG00000083750; Low tissue specificity.
DR MIM; 300725; gene.
DR neXtProt; NX_Q5VZM2; -.
DR OpenTargets; ENSG00000083750; -.
DR PharmGKB; PA134902397; -.
DR VEuPathDB; HostDB:ENSG00000083750; -.
DR eggNOG; KOG3886; Eukaryota.
DR GeneTree; ENSGT00950000183031; -.
DR HOGENOM; CLU_044099_1_0_1; -.
DR InParanoid; Q5VZM2; -.
DR OMA; LIPNMQD; -.
DR OrthoDB; 951213at2759; -.
DR PhylomeDB; Q5VZM2; -.
DR TreeFam; TF300616; -.
DR PathwayCommons; Q5VZM2; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-165159; MTOR signalling.
DR Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q5VZM2; -.
DR SIGNOR; Q5VZM2; -.
DR BioGRID-ORCS; 10325; 13 hits in 712 CRISPR screens.
DR ChiTaRS; RRAGB; human.
DR GeneWiki; RRAGB; -.
DR GenomeRNAi; 10325; -.
DR Pharos; Q5VZM2; Tbio.
DR PRO; PR:Q5VZM2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5VZM2; protein.
DR Bgee; ENSG00000083750; Expressed in calcaneal tendon and 117 other tissues.
DR ExpressionAtlas; Q5VZM2; baseline and differential.
DR Genevisible; Q5VZM2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:HGNC-UCL.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0051020; F:GTPase binding; IPI:CAFA.
DR GO; GO:0032561; F:guanyl ribonucleotide binding; IDA:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IGI:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
DR GO; GO:1990253; P:cellular response to leucine starvation; IMP:CAFA.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:CAFA.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0032006; P:regulation of TOR signaling; IGI:UniProtKB.
DR CDD; cd11384; RagA_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039397; RagA/B.
DR PANTHER; PTHR11259; PTHR11259; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; GTP-binding; Hydrolase;
KW Isopeptide bond; Lysosome; Nucleotide-binding; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..374
FT /note="Ras-related GTP-binding protein B"
FT /id="PRO_0000239948"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
FT BINDING 123..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
FT BINDING 188..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7L523"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7L523"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7L523"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q7L523"
FT VAR_SEQ 77..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:7499430, ECO:0000303|PubMed:9394008"
FT /id="VSP_052073"
FT MUTAGEN 54
FT /note="T->L: Decreased RPTOR-binding."
FT /evidence="ECO:0000269|PubMed:18497260"
FT MUTAGEN 54
FT /note="T->N: Reduced affinity for all nucleotides, but with
FT preferential binding of GDP over GTP."
FT /evidence="ECO:0000269|PubMed:24095279"
FT MUTAGEN 127
FT /note="Q->L: Maintains GTP-bound state. Increased RPTOR-
FT binding."
FT /evidence="ECO:0000269|PubMed:18497260,
FT ECO:0000269|PubMed:24095279"
FT CONFLICT 337
FT /note="M -> V (in Ref. 1; CAA62132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 43250 MW; 0D32F7D86E2A00DE CRC64;
MEESDSEKTT EKENLGPRMD PPLGEPEGSL GWVLPNTAMK KKVLLMGKSG SGKTSMRSII
FANYIARDTR RLGATILDRI HSLQINSSLS TYSLVDSVGN TKTFDVEHSH VRFLGNLVLN
LWDCGGQDTF MENYFTSQRD NIFRNVEVLI YVFDVESREL EKDMHYYQSC LEAILQNSPD
AKIFCLVHKM DLVQEDQRDL IFKEREEDLR RLSRPLECSC FRTSIWDETL YKAWSSIVYQ
LIPNVQQLEM NLRNFAEIIE ADEVLLFERA TFLVISHYQC KEQRDAHRFE KISNIIKQFK
LSCSKLAASF QSMEVRNSNF AAFIDIFTSN TYVMVVMSDP SIPSAATLIN IRNARKHFEK
LERVDGPKQC LLMR
