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Protein

Ragulator complex protein LAMTOR2

Gene

Lamtor2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-165159. mTOR signalling.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-MMU-5628897. TP53 Regulates Metabolic Genes.
R-MMU-5674135. MAP2K and MAPK activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ragulator complex protein LAMTOR2
Alternative name(s):
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
Gene namesi
Name:Lamtor2
Synonyms:Mapbpip, Robld3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1932697. Lamtor2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • late endosome Source: UniProtKB
  • lysosomal membrane Source: MGI
  • Ragulator complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 125125Ragulator complex protein LAMTOR2PRO_0000220961Add
BLAST

Proteomic databases

EPDiQ9JHS3.
MaxQBiQ9JHS3.
PaxDbiQ9JHS3.
PRIDEiQ9JHS3.

PTM databases

iPTMnetiQ9JHS3.
PhosphoSiteiQ9JHS3.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9JHS3.
ExpressionAtlasiQ9JHS3. baseline and differential.
GenevisibleiQ9JHS3. MM.

Interactioni

Subunit structurei

Part of the Ragulator complex composed of LAMTOR1, LAMTOR2, LAMTOR3, LAMTOR4 and LAMTOR5. LAMTOR4 and LAMTOR5 form a heterodimer that interacts, through LAMTOR1, with a LAMTOR2, LAMTOR3 heterodimer. 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:15016825, PubMed:15263099, PubMed:15740743, PubMed:19177150). The Ragulator complex interacts with SLC38A9; the probable amino acid sensor (By similarity). Interacts with LAMTOR1 and LAMTOR3; the interaction is direct. Interacts with MAPK1 and MAP2K1 (PubMed:11266467).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Lamtor1Q6P7914EBI-1038198,EBI-919067From a different organism.
Lamtor3O886532EBI-1038198,EBI-1039530

Protein-protein interaction databases

BioGridi219917. 1 interaction.
IntActiQ9JHS3. 4 interactions.
STRINGi10090.ENSMUSP00000029698.

Structurei

Secondary structure

1
125
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Beta strandi15 – 184Combined sources
Beta strandi19 – 257Combined sources
Turni27 – 293Combined sources
Beta strandi31 – 366Combined sources
Beta strandi38 – 403Combined sources
Helixi42 – 6019Combined sources
Turni63 – 653Combined sources
Beta strandi71 – 766Combined sources
Beta strandi79 – 868Combined sources
Beta strandi89 – 957Combined sources
Helixi101 – 11616Combined sources
Helixi118 – 1203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKOX-ray2.00B2-124[»]
1SZVNMR-A1-125[»]
1VETX-ray1.90B1-125[»]
1VEUX-ray2.15B1-125[»]
2ZL1X-ray2.00B2-125[»]
3CPTX-ray1.90B2-125[»]
ProteinModelPortaliQ9JHS3.
SMRiQ9JHS3. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHS3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 7014Required for location at endosomesAdd
BLAST

Sequence similaritiesi

Belongs to the GAMAD family.Curated

Phylogenomic databases

eggNOGiKOG4107. Eukaryota.
ENOG4111GWH. LUCA.
GeneTreeiENSGT00390000006100.
HOVERGENiHBG004518.
InParanoidiQ9JHS3.
OMAiCECGHVA.
OrthoDBiEOG77DJ8B.
PhylomeDBiQ9JHS3.
TreeFamiTF313929.

Family and domain databases

InterProiIPR004942. Roadblock/LAMTOR2_dom.
[Graphical view]
PfamiPF03259. Robl_LC7. 1 hit.
[Graphical view]
SMARTiSM00960. Robl_LC7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JHS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRPKALTQV LSQANTGGVQ STLLLNNEGS LLAYSGYGDT DARVTAAIAS
60 70 80 90 100
NIWAAYDRNG NQAFNEDSLK FILMDCMEGR VAITRVANLL LCMYAKETVG
110 120
FGMLKAKAQA LVQYLEEPLT QVAAS
Length:125
Mass (Da):13,480
Last modified:October 1, 2000 - v1
Checksum:i69448F11DFD6C03D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ277386 mRNA. Translation: CAB97177.1.
AK019006 mRNA. Translation: BAB31506.1.
BC031816 mRNA. Translation: AAH31816.1.
CCDSiCCDS17478.1.
RefSeqiNP_112538.1. NM_031248.3.
UniGeneiMm.41680.

Genome annotation databases

EnsembliENSMUST00000029698; ENSMUSP00000029698; ENSMUSG00000028062.
GeneIDi83409.
KEGGimmu:83409.
UCSCiuc008pvo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ277386 mRNA. Translation: CAB97177.1.
AK019006 mRNA. Translation: BAB31506.1.
BC031816 mRNA. Translation: AAH31816.1.
CCDSiCCDS17478.1.
RefSeqiNP_112538.1. NM_031248.3.
UniGeneiMm.41680.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SKOX-ray2.00B2-124[»]
1SZVNMR-A1-125[»]
1VETX-ray1.90B1-125[»]
1VEUX-ray2.15B1-125[»]
2ZL1X-ray2.00B2-125[»]
3CPTX-ray1.90B2-125[»]
ProteinModelPortaliQ9JHS3.
SMRiQ9JHS3. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219917. 1 interaction.
IntActiQ9JHS3. 4 interactions.
STRINGi10090.ENSMUSP00000029698.

PTM databases

iPTMnetiQ9JHS3.
PhosphoSiteiQ9JHS3.

Proteomic databases

EPDiQ9JHS3.
MaxQBiQ9JHS3.
PaxDbiQ9JHS3.
PRIDEiQ9JHS3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029698; ENSMUSP00000029698; ENSMUSG00000028062.
GeneIDi83409.
KEGGimmu:83409.
UCSCiuc008pvo.1. mouse.

Organism-specific databases

CTDi28956.
MGIiMGI:1932697. Lamtor2.

Phylogenomic databases

eggNOGiKOG4107. Eukaryota.
ENOG4111GWH. LUCA.
GeneTreeiENSGT00390000006100.
HOVERGENiHBG004518.
InParanoidiQ9JHS3.
OMAiCECGHVA.
OrthoDBiEOG77DJ8B.
PhylomeDBiQ9JHS3.
TreeFamiTF313929.

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.
R-MMU-165159. mTOR signalling.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-MMU-5628897. TP53 Regulates Metabolic Genes.
R-MMU-5674135. MAP2K and MAPK activation.

Miscellaneous databases

EvolutionaryTraceiQ9JHS3.
PROiQ9JHS3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHS3.
ExpressionAtlasiQ9JHS3. baseline and differential.
GenevisibleiQ9JHS3. MM.

Family and domain databases

InterProiIPR004942. Roadblock/LAMTOR2_dom.
[Graphical view]
PfamiPF03259. Robl_LC7. 1 hit.
[Graphical view]
SMARTiSM00960. Robl_LC7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment."
    Wunderlich W., Fialka I., Teis D., Alpi A., Pfeifer A., Parton R.G., Lottspeich F., Huber L.A.
    J. Cell Biol. 152:765-776(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH LAMTOR3; MAPK1 AND MAP2K1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas.
  3. "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].
    Strain: FVB/N.
    Tissue: Salivary gland.
  4. "The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes."
    Nada S., Hondo A., Kasai A., Koike M., Saito K., Uchiyama Y., Okada M.
    EMBO J. 28:477-489(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 97-105, INTERACTION WITH LAMTOR1, SUBCELLULAR LOCATION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal MAP kinase signaling."
    Lunin V.V., Munger C., Wagner J., Ye Z., Cygler M., Sacher M.
    J. Biol. Chem. 279:23422-23430(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-124 IN COMPLEX WITH LAMTOR3.
  7. "Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes."
    Kurzbauer R., Teis D., de Araujo M.E.G., Maurer-Stroh S., Eisenhaber F., Bourenkov G.P., Bartunik H.D., Hekman M., Rapp U.R., Huber L.A., Clausen T.
    Proc. Natl. Acad. Sci. U.S.A. 101:10984-10989(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH LAMTOR3, FUNCTION, SUBCELLULAR LOCATION.
  8. "Structure of the adaptor protein p14 reveals a profilin-like fold with distinct function."
    Qian C., Zhang Q., Wang X., Zeng L., Farooq A., Zhou M.-M.
    J. Mol. Biol. 347:309-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, INTERACTION WITH LAMTOR3.

Entry informationi

Entry nameiLTOR2_MOUSE
AccessioniPrimary (citable) accession number: Q9JHS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.