LTOR2_HUMAN
ID LTOR2_HUMAN Reviewed; 125 AA.
AC Q9Y2Q5; Q5VY97; Q5VY98; Q5VY99;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Ragulator complex protein LAMTOR2;
DE AltName: Full=Endosomal adaptor protein p14;
DE AltName: Full=Late endosomal/lysosomal Mp1-interacting protein;
DE AltName: Full=Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2;
DE AltName: Full=Mitogen-activated protein-binding protein-interacting protein;
DE Short=MAPBP-interacting protein;
DE AltName: Full=Roadblock domain-containing protein 3;
GN Name=LAMTOR2; Synonyms=MAPBPIP, ROBLD3; ORFNames=HSPC003;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [6]
RP INVOLVEMENT IN IMMUNODEFICIENCY DUE TO DEFECT IN MAPBP-INTERACTING PROTEIN.
RX PubMed=17195838; DOI=10.1038/nm1528;
RA Bohn G., Allroth A., Brandes G., Thiel J., Glocker E., Schaeffer A.A.,
RA Rathinam C., Taub N., Teis D., Zeidler C., Dewey R.A., Geffers R., Buer J.,
RA Huber L.A., Welte K., Grimbacher B., Klein C.;
RT "A novel human primary immunodeficiency syndrome caused by deficiency of
RT the endosomal adaptor protein p14.";
RL Nat. Med. 13:38-45(2007).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN RAGULATOR COMPLEX.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION IN MTORC1 SIGNALING, IDENTIFICATION IN RAGULATOR COMPLEX, AND
RP INTERACTION WITH MTORC1 COMPLEX AND RAG GTPASES.
RX PubMed=22980980; DOI=10.1016/j.cell.2012.07.032;
RA Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M.;
RT "Ragulator is a GEF for the Rag GTPases that signal amino acid levels to
RT mTORC1.";
RL Cell 150:1196-1208(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
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).
RN [14] {ECO:0007744|PDB:6ULG}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) IN COMPLEX WITH FLCN;
RP FNIP2; RRAGA; RRAGC; LAMTOR1; LAMTOR3; LAMTOR4 AND LAMTOR5, AND
RP IDENTIFICATION IN THE LFC COMPLEX.
RX PubMed=31704029; DOI=10.1016/j.cell.2019.10.036;
RA Shen K., Rogala K.B., Chou H.T., Huang R.K., Yu Z., Sabatini D.M.;
RT "Cryo-EM structure of the human FLCN-FNIP2-Rag-Ragulator complex.";
RL Cell 179:1319-1329(2019).
RN [15] {ECO:0007744|PDB:6NZD}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH FLCN;
RP FNIP2; RRAGA; RRAGC; LAMTOR1; LAMTOR3; LAMTOR4 AND LAMTOR5, AND
RP IDENTIFICATION IN THE LFC COMPLEX.
RX PubMed=31672913; DOI=10.1126/science.aax0364;
RA Lawrence R.E., Fromm S.A., Fu Y., Yokom A.L., Kim D.J., Thelen A.M.,
RA Young L.N., Lim C.Y., Samelson A.J., Hurley J.H., Zoncu R.;
RT "Structural mechanism of a Rag GTPase activation checkpoint by the
RT lysosomal folliculin complex.";
RL Science 366:971-977(2019).
CC -!- FUNCTION: As part of the Ragulator complex it is involved in amino acid
CC sensing and activation of mTORC1, a signaling complex promoting cell
CC growth in response to growth factors, energy levels, and amino acids.
CC Activated by amino acids through a mechanism involving the lysosomal V-
CC ATPase, the Ragulator functions as a guanine nucleotide exchange factor
CC activating the small GTPases Rag. Activated Ragulator and Rag GTPases
CC function as a scaffold recruiting mTORC1 to lysosomes where it is in
CC turn activated. Adapter protein that enhances the efficiency of the MAP
CC kinase cascade facilitating the activation of MAPK2.
CC {ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980}.
CC -!- SUBUNIT: Part of the Ragulator complex composed of LAMTOR1, LAMTOR2,
CC LAMTOR3, LAMTOR4 and LAMTOR5 (PubMed:20381137, PubMed:22980980).
CC LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1,
CC with a LAMTOR2, LAMTOR3 heterodimer (PubMed:20381137, PubMed:22980980).
CC Interacts with LAMTOR1 and LAMTOR3; the interaction is direct
CC (PubMed:20381137, PubMed:22980980). The Ragulator complex interacts
CC with both the mTORC1 complex and heterodimers constituted of the Rag
CC GTPases RRAGA, RRAGB, RRAGC and RRAGD; regulated by amino acid
CC availability (PubMed:20381137, PubMed:22980980). The Ragulator complex
CC interacts with SLC38A9; the probable amino acid sensor
CC (PubMed:25561175, PubMed:25567906). Interacts with MAPK1 and MAP2K1 (By
CC similarity). Component of the lysosomal folliculin complex (LFC),
CC composed of FLCN, FNIP1 (or FNIP2), RRAGA/RagA or RRAGB/RagB GDP-bound,
CC RRAGC/RagC or RRAGD/RagD GTP-bound, and Ragulator (PubMed:31704029,
CC PubMed:31672913). {ECO:0000250|UniProtKB:Q9JHS3,
CC ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:22980980,
CC ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906,
CC ECO:0000269|PubMed:31672913, ECO:0000269|PubMed:31704029}.
CC -!- INTERACTION:
CC Q9Y2Q5; Q96GS4: BORCS6; NbExp=4; IntAct=EBI-2643704, EBI-10193358;
CC Q9Y2Q5; Q6IAA8: LAMTOR1; NbExp=14; IntAct=EBI-2643704, EBI-715385;
CC Q9Y2Q5; Q9UHA4: LAMTOR3; NbExp=18; IntAct=EBI-2643704, EBI-1038192;
CC Q9Y2Q5; Q8NBW4: SLC38A9; NbExp=3; IntAct=EBI-2643704, EBI-9978316;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Lysosome membrane {ECO:0000269|PubMed:17897319}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2Q5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2Q5-2; Sequence=VSP_036543;
CC Name=3;
CC IsoId=Q9Y2Q5-3; Sequence=VSP_040980;
CC -!- DISEASE: Immunodeficiency due to defect in MAPBP-interacting protein
CC (ID-MAPBPIP) [MIM:610798]: This form of primary immunodeficiency
CC syndrome includes congenital neutropenia, partial albinism, short
CC stature and B-cell and cytotoxic T-cell deficiency.
CC {ECO:0000269|PubMed:17195838}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the GAMAD family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=MAPBPIPbase; Note=ROBLD3 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/MAPBPIPbase/";
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DR EMBL; AF070659; AAD20965.1; -; mRNA.
DR EMBL; AK307086; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL355388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024190; AAH24190.1; -; mRNA.
DR CCDS; CCDS1128.1; -. [Q9Y2Q5-1]
DR CCDS; CCDS44243.1; -. [Q9Y2Q5-3]
DR RefSeq; NP_001138736.1; NM_001145264.1. [Q9Y2Q5-3]
DR RefSeq; NP_054736.1; NM_014017.3. [Q9Y2Q5-1]
DR PDB; 5X6U; X-ray; 2.40 A; B=1-125.
DR PDB; 5X6V; X-ray; 2.02 A; B=1-125.
DR PDB; 5Y39; X-ray; 2.65 A; B/G=1-125.
DR PDB; 5Y3A; X-ray; 2.90 A; B/G=1-125.
DR PDB; 6B9X; X-ray; 1.42 A; B=1-125.
DR PDB; 6EHP; X-ray; 2.30 A; B=2-125.
DR PDB; 6EHR; X-ray; 2.90 A; B=2-125.
DR PDB; 6NZD; EM; 3.60 A; B=1-125.
DR PDB; 6U62; EM; 3.18 A; E=1-125.
DR PDB; 6ULG; EM; 3.31 A; B=1-125.
DR PDB; 6WJ2; EM; 3.20 A; B=1-125.
DR PDB; 6WJ3; EM; 3.90 A; B=1-125.
DR PDB; 7T3A; EM; 4.00 A; N=1-125.
DR PDB; 7T3B; EM; 3.90 A; G=1-125.
DR PDB; 7T3C; EM; 4.00 A; G/N=1-125.
DR PDBsum; 5X6U; -.
DR PDBsum; 5X6V; -.
DR PDBsum; 5Y39; -.
DR PDBsum; 5Y3A; -.
DR PDBsum; 6B9X; -.
DR PDBsum; 6EHP; -.
DR PDBsum; 6EHR; -.
DR PDBsum; 6NZD; -.
DR PDBsum; 6U62; -.
DR PDBsum; 6ULG; -.
DR PDBsum; 6WJ2; -.
DR PDBsum; 6WJ3; -.
DR PDBsum; 7T3A; -.
DR PDBsum; 7T3B; -.
DR PDBsum; 7T3C; -.
DR AlphaFoldDB; Q9Y2Q5; -.
DR BMRB; Q9Y2Q5; -.
DR SMR; Q9Y2Q5; -.
DR BioGRID; 118783; 105.
DR ComplexPortal; CPX-4741; Ragulator complex.
DR CORUM; Q9Y2Q5; -.
DR DIP; DIP-57000N; -.
DR IntAct; Q9Y2Q5; 19.
DR MINT; Q9Y2Q5; -.
DR STRING; 9606.ENSP00000357288; -.
DR iPTMnet; Q9Y2Q5; -.
DR PhosphoSitePlus; Q9Y2Q5; -.
DR SwissPalm; Q9Y2Q5; -.
DR BioMuta; LAMTOR2; -.
DR DMDM; 12585246; -.
DR OGP; Q9Y2Q5; -.
DR EPD; Q9Y2Q5; -.
DR jPOST; Q9Y2Q5; -.
DR MassIVE; Q9Y2Q5; -.
DR MaxQB; Q9Y2Q5; -.
DR PaxDb; Q9Y2Q5; -.
DR PeptideAtlas; Q9Y2Q5; -.
DR PRIDE; Q9Y2Q5; -.
DR ProteomicsDB; 85869; -. [Q9Y2Q5-1]
DR ProteomicsDB; 85870; -. [Q9Y2Q5-2]
DR ProteomicsDB; 85871; -. [Q9Y2Q5-3]
DR TopDownProteomics; Q9Y2Q5-1; -. [Q9Y2Q5-1]
DR TopDownProteomics; Q9Y2Q5-2; -. [Q9Y2Q5-2]
DR TopDownProteomics; Q9Y2Q5-3; -. [Q9Y2Q5-3]
DR Antibodypedia; 1218; 101 antibodies from 25 providers.
DR DNASU; 28956; -.
DR Ensembl; ENST00000368302.3; ENSP00000357285.3; ENSG00000116586.12. [Q9Y2Q5-2]
DR Ensembl; ENST00000368304.9; ENSP00000357287.5; ENSG00000116586.12. [Q9Y2Q5-3]
DR Ensembl; ENST00000368305.9; ENSP00000357288.4; ENSG00000116586.12. [Q9Y2Q5-1]
DR GeneID; 28956; -.
DR KEGG; hsa:28956; -.
DR MANE-Select; ENST00000368305.9; ENSP00000357288.4; NM_014017.4; NP_054736.1.
DR UCSC; uc001fnb.4; human. [Q9Y2Q5-1]
DR CTD; 28956; -.
DR DisGeNET; 28956; -.
DR GeneCards; LAMTOR2; -.
DR HGNC; HGNC:29796; LAMTOR2.
DR HPA; ENSG00000116586; Low tissue specificity.
DR MalaCards; LAMTOR2; -.
DR MIM; 610389; gene.
DR MIM; 610798; phenotype.
DR neXtProt; NX_Q9Y2Q5; -.
DR OpenTargets; ENSG00000116586; -.
DR Orphanet; 90023; Primary immunodeficiency syndrome due to LAMTOR2 deficiency.
DR PharmGKB; PA164725527; -.
DR VEuPathDB; HostDB:ENSG00000116586; -.
DR eggNOG; KOG4107; Eukaryota.
DR GeneTree; ENSGT00390000006100; -.
DR HOGENOM; CLU_141118_0_0_1; -.
DR InParanoid; Q9Y2Q5; -.
DR OMA; WAAYEKN; -.
DR OrthoDB; 1515483at2759; -.
DR PhylomeDB; Q9Y2Q5; -.
DR TreeFam; TF313929; -.
DR PathwayCommons; Q9Y2Q5; -.
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-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q9Y2Q5; -.
DR SIGNOR; Q9Y2Q5; -.
DR BioGRID-ORCS; 28956; 413 hits in 1091 CRISPR screens.
DR ChiTaRS; LAMTOR2; human.
DR GenomeRNAi; 28956; -.
DR Pharos; Q9Y2Q5; Tbio.
DR PRO; PR:Q9Y2Q5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y2Q5; protein.
DR Bgee; ENSG00000116586; Expressed in mucosa of transverse colon and 186 other tissues.
DR Genevisible; Q9Y2Q5; HS.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IC:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0071986; C:Ragulator complex; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:ComplexPortal.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:1902414; P:protein localization to cell junction; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0150116; P:regulation of cell-substrate junction organization; IMP:MGI.
DR GO; GO:0038202; P:TORC1 signaling; IC:ComplexPortal.
DR InterPro; IPR037587; LAMTOR2-like.
DR InterPro; IPR004942; Roadblock/LAMTOR2_dom.
DR PANTHER; PTHR13323; PTHR13323; 1.
DR Pfam; PF03259; Robl_LC7; 1.
DR SMART; SM00960; Robl_LC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endosome; Lysosome; Membrane;
KW Reference proteome.
FT CHAIN 1..125
FT /note="Ragulator complex protein LAMTOR2"
FT /id="PRO_0000220960"
FT REGION 57..70
FT /note="Required for location at endosomes"
FT /evidence="ECO:0000250"
FT VAR_SEQ 78..107
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040980"
FT VAR_SEQ 109..125
FT /note="QALVQYLEEPLTQVAAS -> VCGTDLCSPSAGPGFGAVPGGAPHPSGGILT
FT ALVEAGVRKEK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036543"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5X6U"
FT HELIX 42..60
FT /evidence="ECO:0007829|PDB:6B9X"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5X6V"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:6B9X"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:6B9X"
FT HELIX 101..122
FT /evidence="ECO:0007829|PDB:6B9X"
SQ SEQUENCE 125 AA; 13508 MW; 69599211C2CBC03D CRC64;
MLRPKALTQV LSQANTGGVQ STLLLNNEGS LLAYSGYGDT DARVTAAIAS NIWAAYDRNG
NQAFNEDNLK FILMDCMEGR VAITRVANLL LCMYAKETVG FGMLKAKAQA LVQYLEEPLT
QVAAS
