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Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1) (Lipid raft adaptor protein p18) (Protein associated with DRMs and endosomes) (p27Kip1-releasing factor from RhoA) (p27RF-Rho)

 LTOR1_HUMAN             Reviewed;         161 AA.
Q6IAA8; Q8WZ09; Q9NWT0;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
12-AUG-2020, entry version 139.
RecName: Full=Ragulator complex protein LAMTOR1;
AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1;
AltName: Full=Lipid raft adaptor protein p18;
AltName: Full=Protein associated with DRMs and endosomes;
AltName: Full=p27Kip1-releasing factor from RhoA;
Short=p27RF-Rho;
Name=LAMTOR1; Synonyms=C11orf59, PDRO; ORFNames=PP7157;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[5]
PROTEIN SEQUENCE OF 48-60 AND 135-147, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MMP14 AND CDKN1B.
PubMed=19654316; DOI=10.1074/jbc.m109.041400;
Hoshino D., Tomari T., Nagano M., Koshikawa N., Seiki M.;
"A novel protein associated with membrane-type 1 matrix metalloproteinase
binds p27(kip1) and regulates RhoA activation, actin remodeling, and
matrigel invasion.";
J. Biol. Chem. 284:27315-27326(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
FUNCTION, IDENTIFICATION IN RAGULATOR COMPLEX, AND INTERACTION WITH RRAGB
AND RRAGD.
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]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY CHOLESTEROL.
PubMed=20544018; DOI=10.1371/journal.pone.0010977;
Guillaumot P., Luquain C., Malek M., Huber A.L., Brugiere S., Garin J.,
Grunwald D., Regnier D., Petrilli V., Lefai E., Manie S.N.;
"Pdro, a protein associated with late endosomes and lysosomes and
implicated in cellular cholesterol homeostasis.";
PLoS ONE 5:E10977-E10977(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
FUNCTION IN MTORC1 SIGNALING, IDENTIFICATION IN RAGULATOR COMPLEX, AND
INTERACTION WITH MTORC1 COMPLEX AND RAG GTPASES.
PubMed=22980980; DOI=10.1016/j.cell.2012.07.032;
Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M.;
"Ragulator is a GEF for the Rag GTPases that signal amino acid levels to
mTORC1.";
Cell 150:1196-1208(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-42; SER-56; SER-98
AND SER-141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated proteomes
in human cells.";
Nat. Commun. 5:4919-4919(2014).
[19]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
[20]
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).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
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).
[23]
INTERACTION WITH PIP4P1.
PubMed=29644770; DOI=10.1111/gtc.12583;
Hashimoto Y., Shirane M., Nakayama K.I.;
"TMEM55B contributes to lysosomal homeostasis and amino acid-induced mTORC1
activation.";
Genes Cells 23:418-434(2018).
[24] {ECO:0000244|PDB:6ULG}
STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) IN COMPLEX WITH FLCN;
FNIP2; RRAGA; RRAGC; LAMTOR2; LAMTOR3; LAMTOR4 AND LAMTOR5, AND
IDENTIFICATION IN THE LFC COMPLEX.
PubMed=31704029; DOI=10.1016/j.cell.2019.10.036;
Shen K., Rogala K.B., Chou H.T., Huang R.K., Yu Z., Sabatini D.M.;
"Cryo-EM structure of the human FLCN-FNIP2-Rag-Ragulator complex.";
Cell 179:1319-1329(2019).
[25] {ECO:0000244|PDB:6NZD}
STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 5-161 IN COMPLEX WITH
FLCN; FNIP2; RRAGA; RRAGC; LAMTOR2; LAMTOR3; LAMTOR4 AND LAMTOR5, AND
IDENTIFICATION IN THE LFC COMPLEX.
PubMed=31672913; DOI=10.1126/science.aax0364;
Lawrence R.E., Fromm S.A., Fu Y., Yokom A.L., Kim D.J., Thelen A.M.,
Young L.N., Lim C.Y., Samelson A.J., Hurley J.H., Zoncu R.;
"Structural mechanism of a Rag GTPase activation checkpoint by the
lysosomal folliculin complex.";
Science 366:971-977(2019).
-!- FUNCTION: As part of the Ragulator complex it is involved in amino acid
sensing and activation of mTORC1, a signaling complex promoting cell
growth in response to growth factors, energy levels, and amino acids.
Activated by amino acids through a mechanism involving the lysosomal V-
ATPase, the Ragulator functions as a guanine nucleotide exchange factor
activating the small GTPases Rag. Activated Ragulator and Rag GTPases
function as a scaffold recruiting mTORC1 to lysosomes where it is in
turn activated. LAMTOR1 is directly responsible for anchoring the
Ragulator complex to membranes. Also required for late
endosomes/lysosomes biogenesis it may regulate both the recycling of
receptors through endosomes and the MAPK signaling pathway through
recruitment of some of its components to late endosomes. May be
involved in cholesterol homeostasis regulating LDL uptake and
cholesterol release from late endosomes/lysosomes. May also play a role
in RHOA activation. {ECO:0000269|PubMed:19654316,
ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:20544018,
ECO:0000269|PubMed:22980980}.
-!- SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, LAMTOR2,
LAMTOR3, LAMTOR4 and LAMTOR5 (PubMed:20381137, PubMed:22980980).
LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1,
with a LAMTOR2, LAMTOR3 heterodimer (PubMed:20381137, PubMed:22980980).
Interacts with LAMTOR2 and LAMTOR3; the interaction is direct
(PubMed:20381137, PubMed:22980980). The Ragulator complex interacts
with both the mTORC1 complex and heterodimers constituted of the Rag
GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid
availability (PubMed:20381137, PubMed:22980980). The Ragulator complex
interacts with SLC38A9; the probable amino acid sensor
(PubMed:25561175, PubMed:25567906). Component of the lysosomal
folliculin complex (LFC), composed of FLCN, FNIP1 (or FNIP2),
RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD GTP-bound,
and Ragulator (PubMed:31704029, PubMed:31672913). Interacts with RRAGB
and RRAGD; the interaction is direct indicating that it probably
constitutes the main RAG-interacting subunit of the Ragulator complex
(PubMed:22980980). Interacts with MMP14 (PubMed:19654316). Interacts
with CDKN1B; prevents the interaction of CDKN1B with RHOA leaving RHOA
in a form accessible to activation by ARHGEF2 (PubMed:19654316).
Interacts with PIP4P1 (PubMed:29644770). {ECO:0000269|PubMed:19654316,
ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980,
ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906,
ECO:0000269|PubMed:29644770, ECO:0000269|PubMed:31672913,
ECO:0000269|PubMed:31704029}.
-!- INTERACTION:
Q6IAA8; P78358: CTAG1B; NbExp=3; IntAct=EBI-715385, EBI-1188472;
Q6IAA8; Q9Y2Q5: LAMTOR2; NbExp=14; IntAct=EBI-715385, EBI-2643704;
Q6IAA8; Q7L523: RRAGA; NbExp=11; IntAct=EBI-715385, EBI-752376;
Q6IAA8; Q8NBW4: SLC38A9; NbExp=12; IntAct=EBI-715385, EBI-9978316;
-!- SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor; Cytoplasmic
side. Lysosome membrane {ECO:0000269|PubMed:20544018}; Lipid-anchor;
Cytoplasmic side. Cell membrane.
-!- INDUCTION: Down-regulated by cholesterol (at protein level).
{ECO:0000269|PubMed:20544018}.
-!- SIMILARITY: Belongs to the LAMTOR1 family. {ECO:0000305}.
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EMBL; AF289583; AAL55767.1; -; mRNA.
EMBL; CR457247; CAG33528.1; -; mRNA.
EMBL; AK000632; BAA91297.1; -; mRNA.
EMBL; BC001706; AAH01706.1; -; mRNA.
CCDS; CCDS8209.1; -.
RefSeq; NP_060377.1; NM_017907.2.
PDB; 5X6U; X-ray; 2.40 A; E=42-161.
PDB; 5X6V; X-ray; 2.02 A; E=42-161.
PDB; 5Y39; X-ray; 2.65 A; A/F=76-145.
PDB; 5Y3A; X-ray; 2.90 A; A/F=50-161.
PDB; 6B9X; X-ray; 1.42 A; A=1-161.
PDB; 6EHP; X-ray; 2.30 A; E=21-161.
PDB; 6EHR; X-ray; 2.90 A; E=21-161.
PDB; 6NZD; EM; 3.60 A; A=5-161.
PDB; 6U62; EM; 3.18 A; D=6-161.
PDB; 6ULG; EM; 3.31 A; E=1-161.
PDBsum; 5X6U; -.
PDBsum; 5X6V; -.
PDBsum; 5Y39; -.
PDBsum; 5Y3A; -.
PDBsum; 6B9X; -.
PDBsum; 6EHP; -.
PDBsum; 6EHR; -.
PDBsum; 6NZD; -.
PDBsum; 6U62; -.
PDBsum; 6ULG; -.
SMR; Q6IAA8; -.
BioGRID; 120336; 73.
ComplexPortal; CPX-4741; Ragulator complex.
CORUM; Q6IAA8; -.
DIP; DIP-39650N; -.
IntAct; Q6IAA8; 41.
MINT; Q6IAA8; -.
STRING; 9606.ENSP00000278671; -.
iPTMnet; Q6IAA8; -.
PhosphoSitePlus; Q6IAA8; -.
SwissPalm; Q6IAA8; -.
BioMuta; LAMTOR1; -.
DMDM; 125863645; -.
EPD; Q6IAA8; -.
jPOST; Q6IAA8; -.
MassIVE; Q6IAA8; -.
MaxQB; Q6IAA8; -.
PaxDb; Q6IAA8; -.
PeptideAtlas; Q6IAA8; -.
PRIDE; Q6IAA8; -.
ProteomicsDB; 66364; -.
TopDownProteomics; Q6IAA8; -.
Antibodypedia; 721; 75 antibodies.
Ensembl; ENST00000278671; ENSP00000278671; ENSG00000149357.
GeneID; 55004; -.
KEGG; hsa:55004; -.
UCSC; uc001ort.3; human.
CTD; 55004; -.
DisGeNET; 55004; -.
EuPathDB; HostDB:ENSG00000149357.9; -.
GeneCards; LAMTOR1; -.
HGNC; HGNC:26068; LAMTOR1.
HPA; ENSG00000149357; Low tissue specificity.
MIM; 613510; gene.
neXtProt; NX_Q6IAA8; -.
OpenTargets; ENSG00000149357; -.
PharmGKB; PA143485354; -.
eggNOG; ENOG502RYX2; Eukaryota.
GeneTree; ENSGT00390000016789; -.
HOGENOM; CLU_136283_1_0_1; -.
InParanoid; Q6IAA8; -.
KO; K20397; -.
OMA; LHETAAN; -.
OrthoDB; 1274244at2759; -.
PhylomeDB; Q6IAA8; -.
TreeFam; TF323788; -.
PathwayCommons; Q6IAA8; -.
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-6798695; Neutrophil degranulation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
SIGNOR; Q6IAA8; -.
BioGRID-ORCS; 55004; 124 hits in 885 CRISPR screens.
ChiTaRS; LAMTOR1; human.
GenomeRNAi; 55004; -.
Pharos; Q6IAA8; Tbio.
PRO; PR:Q6IAA8; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; Q6IAA8; protein.
Bgee; ENSG00000149357; Expressed in muscle tissue and 215 other tissues.
ExpressionAtlas; Q6IAA8; baseline and differential.
Genevisible; Q6IAA8; HS.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0071986; C:Ragulator complex; IDA:UniProtKB.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0051020; F:GTPase binding; IPI:CAFA.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0034613; P:cellular protein localization; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
GO; GO:0010874; P:regulation of cholesterol efflux; IMP:UniProtKB.
GO; GO:0010872; P:regulation of cholesterol esterification; IMP:UniProtKB.
GO; GO:0060620; P:regulation of cholesterol import; IMP:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0001919; P:regulation of receptor recycling; ISS:UniProtKB.
InterPro; IPR028209; LAMTOR1/MEH1.
Pfam; PF15454; LAMTOR; 1.
SMART; SM01262; LAMTOR; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Direct protein sequencing; Endosome;
Lipoprotein; Lysosome; Membrane; Myristate; Phosphoprotein; Polymorphism;
Reference proteome.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930"
CHAIN 2..161
/note="Ragulator complex protein LAMTOR1"
/id="PRO_0000274292"
REGION 121..161
/note="Interaction with LAMTOR2 and LAMTOR3"
/evidence="ECO:0000250"
MOD_RES 27
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163"
MOD_RES 42
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 56
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 98
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 141
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
LIPID 2
/note="N-myristoyl glycine"
/evidence="ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930"
VARIANT 73
/note="S -> L (in dbSNP:rs1053443)"
/id="VAR_030250"
CONFLICT 50
/note="E -> V (in Ref. 2; CAG33528)"
/evidence="ECO:0000305"
CONFLICT 60
/note="K -> R (in Ref. 1; AAL55767)"
/evidence="ECO:0000305"
CONFLICT 69
/note="S -> P (in Ref. 2; CAG33528)"
/evidence="ECO:0000305"
HELIX 50..64
/evidence="ECO:0000244|PDB:5X6V"
TURN 75..77
/evidence="ECO:0000244|PDB:6EHR"
HELIX 78..95
/evidence="ECO:0000244|PDB:5X6V"
HELIX 98..102
/evidence="ECO:0000244|PDB:6B9X"
HELIX 115..120
/evidence="ECO:0000244|PDB:6B9X"
HELIX 126..142
/evidence="ECO:0000244|PDB:6B9X"
HELIX 143..145
/evidence="ECO:0000244|PDB:6B9X"
STRAND 154..156
/evidence="ECO:0000244|PDB:6EHR"
SEQUENCE 161 AA; 17745 MW; 610CC6C548356051 CRC64;
MGCCYSSENE DSDQDREERK LLLDPSSPPT KALNGAEPNY HSLPSARTDE QALLSSILAK
TASNIIDVSA ADSQGMEQHE YMDRARQYST RLAVLSSSLT HWKKLPPLPS LTSQPHQVLA
SEPIPFSDLQ QVSRIAAYAY SALSQIRVDA KEELVVQFGI P


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Catalog number Product name Quantity
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Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP2032: TSH signaling pathway
WP73: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP1502: Mitochondrial biogenesis
WP35: G Protein Signaling Pathways
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways
WP232: G Protein Signaling Pathways
WP1678: Nucleotide excision repair
WP525: Mitochondrial Unfolded-Protein Response
WP1624: Bacterial secretion system
WP1939: Unfolded Protein Response
WP1690: Propanoate metabolism
WP2203: TSLP Signaling Pathway
WP1694: Pyrimidine metabolism
WP1657: Glycerolipid metabolism
WP1371: G Protein Signaling Pathways
WP1663: Homologous recombination
WP1566: Citrate cycle (TCA cycle)
WP1714: Tyrosine metabolism
WP1672: Mismatch repair
WP1676: Non-homologous end-joining

Related Genes :
[LAMTOR1 C11orf59 PDRO PP7157] Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1) (Lipid raft adaptor protein p18) (Protein associated with DRMs and endosomes) (p27Kip1-releasing factor from RhoA) (p27RF-Rho)
[Lamtor1] Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1) (Lipid raft adaptor protein p18)
[Lamtor1] Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1) (Lipid raft adaptor protein p18)
[Lamtor2 Mapbpip Robld3] Ragulator complex protein LAMTOR2 (Endosomal adaptor protein p14) (Late endosomal/lysosomal Mp1-interacting protein) (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2) (Mitogen-activated protein-binding protein-interacting protein) (Roadblock domain-containing protein 3)
[Lamtor3 Map2k1ip1 Mapbp Mapksp1] Ragulator complex protein LAMTOR3 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3) (MEK-binding partner 1) (Mp1) (Mitogen-activated protein kinase kinase 1-interacting protein 1) (Mitogen-activated protein kinase scaffold protein 1)
[LAMTOR2 MAPBPIP ROBLD3 HSPC003] Ragulator complex protein LAMTOR2 (Endosomal adaptor protein p14) (Late endosomal/lysosomal Mp1-interacting protein) (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2) (Mitogen-activated protein-binding protein-interacting protein) (MAPBP-interacting protein) (Roadblock domain-containing protein 3)
[LAMTOR3 MAP2K1IP1 MAPKSP1 PRO2783] Ragulator complex protein LAMTOR3 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3) (MEK-binding partner 1) (Mp1) (Mitogen-activated protein kinase kinase 1-interacting protein 1) (Mitogen-activated protein kinase scaffold protein 1)
[LAMTOR1] Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1)
[LAMTOR1] Ragulator complex protein LAMTOR1 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1)
[LAMTOR4 C7orf59] Ragulator complex protein LAMTOR4 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 4) [Cleaved into: Ragulator complex protein LAMTOR4, N-terminally processed]
[LAMTOR5 HBXIP XIP] Ragulator complex protein LAMTOR5 (Hepatitis B virus X-interacting protein) (HBV X-interacting protein) (HBX-interacting protein) (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5)
[CDKN1B KIP1] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)
[MTOR FRAP FRAP1 FRAP2 RAFT1 RAPT1] Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin and FKBP12 target 1) (Rapamycin target protein 1)
[Lamtor5 Hbxip Xip] Ragulator complex protein LAMTOR5 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5)
[Mtor Frap1 Raft1] Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin target protein 1) (RAPT1)
[Cdkn1b] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)
[LAMTOR2] Ragulator complex protein LAMTOR2 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2)
[Lamtor3 Map2k1ip1] Ragulator complex protein LAMTOR3 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3) (Mitogen-activated protein kinase kinase 1-interacting protein 1)
[CDKN1B KIP1] Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1)
[Map2k1 Mek1 Prkmk1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[Lamtor4] Ragulator complex protein LAMTOR4 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 4) [Cleaved into: Ragulator complex protein LAMTOR4, N-terminally processed]
[Mtor Frap Frap1] Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin target protein 1) (RAPT1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[LAMTOR4] Ragulator complex protein LAMTOR4 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 4) [Cleaved into: Ragulator complex protein LAMTOR4, N-terminally processed]
[GRB2 ASH] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :
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