UniProt ID | LTOR1_MOUSE | |
---|---|---|
UniProt AC | Q9CQ22 | |
Protein Name | Ragulator complex protein LAMTOR1 | |
Gene Name | Lamtor1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 161 | |
Subcellular Localization |
Late endosome membrane Lipid-anchor Cytoplasmic side. Lysosome membrane Lipid-anchor Cytoplasmic side. Cell membrane Lipid-anchor . |
|
Protein Description | 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.. | |
Protein Sequence | MGCCYSSENEDSDQDREERKLLLDPSSTPTKALNGAEPNYHSLPSARTDEQALLSSILAKTASNIIDVSAADSQGMEQHEYMDRARQYSTRLAVLSSSLTHWKKLPPLPSLTSQPHQVLASEPIPFSDLQQVSRIAAYAYSALSQIRVDAKEELVVQFGIP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Myristoylation | ------MGCCYSSEN ------CCCCCCCCC | 15.37 | - | |
20 | Ubiquitination | DQDREERKLLLDPSS CCCHHHHHHHCCCCC | 46.93 | 22790023 | |
26 | Phosphorylation | RKLLLDPSSTPTKAL HHHHCCCCCCCCHHH | 46.65 | 24925903 | |
27 | Phosphorylation | KLLLDPSSTPTKALN HHHCCCCCCCCHHHC | 43.74 | 24925903 | |
28 | Phosphorylation | LLLDPSSTPTKALNG HHCCCCCCCCHHHCC | 39.04 | 24925903 | |
30 | Phosphorylation | LDPSSTPTKALNGAE CCCCCCCCHHHCCCC | 29.10 | 24925903 | |
31 | Ubiquitination | DPSSTPTKALNGAEP CCCCCCCHHHCCCCC | 52.67 | 22790023 | |
40 | Phosphorylation | LNGAEPNYHSLPSAR HCCCCCCCCCCCCCC | 11.96 | 25159016 | |
42 | Phosphorylation | GAEPNYHSLPSARTD CCCCCCCCCCCCCCH | 31.45 | 30635358 | |
45 | Phosphorylation | PNYHSLPSARTDEQA CCCCCCCCCCCHHHH | 35.36 | 30635358 | |
48 | Phosphorylation | HSLPSARTDEQALLS CCCCCCCCHHHHHHH | 43.54 | 27717184 | |
55 | Phosphorylation | TDEQALLSSILAKTA CHHHHHHHHHHHHHH | 19.04 | 26239621 | |
56 | Phosphorylation | DEQALLSSILAKTAS HHHHHHHHHHHHHHH | 22.91 | 26824392 | |
61 | Phosphorylation | LSSILAKTASNIIDV HHHHHHHHHHCCCCH | 29.70 | 27742792 | |
63 | Phosphorylation | SILAKTASNIIDVSA HHHHHHHHCCCCHHH | 33.52 | 25521595 | |
69 | Phosphorylation | ASNIIDVSAADSQGM HHCCCCHHHHHHCCC | 17.62 | - | |
73 | Phosphorylation | IDVSAADSQGMEQHE CCHHHHHHCCCHHHH | 24.73 | - | |
96 | Phosphorylation | STRLAVLSSSLTHWK HHHHHHHHHCCCCHH | 15.98 | 26745281 | |
97 | Phosphorylation | TRLAVLSSSLTHWKK HHHHHHHHCCCCHHH | 25.80 | 26745281 | |
98 | Phosphorylation | RLAVLSSSLTHWKKL HHHHHHHCCCCHHHC | 33.63 | 26745281 | |
100 | Phosphorylation | AVLSSSLTHWKKLPP HHHHHCCCCHHHCCC | 27.86 | 26745281 | |
104 | Ubiquitination | SSLTHWKKLPPLPSL HCCCCHHHCCCCCCC | 62.12 | 27667366 | |
110 | Phosphorylation | KKLPPLPSLTSQPHQ HHCCCCCCCCCCCCE | 52.54 | 26060331 | |
112 | Phosphorylation | LPPLPSLTSQPHQVL CCCCCCCCCCCCEEH | 29.65 | 26060331 | |
113 | Phosphorylation | PPLPSLTSQPHQVLA CCCCCCCCCCCEEHH | 47.19 | 24719451 | |
138 | Phosphorylation | QVSRIAAYAYSALSQ HHHHHHHHHHHHHHC | 9.32 | - | |
140 | Phosphorylation | SRIAAYAYSALSQIR HHHHHHHHHHHHCCC | 5.04 | - | |
141 | Phosphorylation | RIAAYAYSALSQIRV HHHHHHHHHHHCCCC | 17.98 | 27180971 | |
144 | Phosphorylation | AYAYSALSQIRVDAK HHHHHHHHCCCCCCC | 24.23 | 24719451 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of LTOR1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LTOR1_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of LTOR1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of LTOR1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY. | |
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, AND MASSSPECTROMETRY. |