dbPTM

LTOR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LTOR1_HUMAN
UniProt AC	Q6IAA8
Protein Name	Ragulator complex protein LAMTOR1
Gene Name	LAMTOR1
Organism	Homo sapiens (Human).
Sequence Length	161
Subcellular Localization	Late endosome membrane Lipid-anchor Cytoplasmic side. Lysosome membrane Lipid-anchor Cytoplasmic side. Cell membrane.
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	MGCCYSSENEDSDQDREERKLLLDPSSPPTKALNGAEPNYHSLPSARTDEQALLSSILAKTASNIIDVSAADSQGMEQHEYMDRARQYSTRLAVLSSSLTHWKKLPPLPSLTSQPHQVLASEPIPFSDLQQVSRIAAYAYSALSQIRVDAKEELVVQFGIP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGCCYSSEN ------CCCCCCCCC	15.37	25807930
5	Phosphorylation	---MGCCYSSENEDS ---CCCCCCCCCCCC	21.22	24043423
6	Phosphorylation	--MGCCYSSENEDSD --CCCCCCCCCCCCC	19.77	24043423
7	Phosphorylation	-MGCCYSSENEDSDQ -CCCCCCCCCCCCCC	20.26	30576142
12	Phosphorylation	YSSENEDSDQDREER CCCCCCCCCCCHHHH	30.87	24043423
20	Ubiquitination	DQDREERKLLLDPSS CCCHHHHHHHCCCCC	46.93	23000965
26	Phosphorylation	RKLLLDPSSPPTKAL HHHHCCCCCCCCHHC	55.96	29255136
27	Phosphorylation	KLLLDPSSPPTKALN HHHCCCCCCCCHHCC	40.04	29255136
30	Phosphorylation	LDPSSPPTKALNGAE CCCCCCCCHHCCCCC	32.12	30266825
31	Ubiquitination	DPSSPPTKALNGAEP CCCCCCCHHCCCCCC	57.56	23000965
40	Phosphorylation	LNGAEPNYHSLPSAR CCCCCCCCCCCCCCC	11.96	21945579
42	Phosphorylation	GAEPNYHSLPSARTD CCCCCCCCCCCCCCH	31.45	23401153
45	Phosphorylation	PNYHSLPSARTDEQA CCCCCCCCCCCHHHH	35.36	21945579
48	Phosphorylation	HSLPSARTDEQALLS CCCCCCCCHHHHHHH	43.54	26657352
55	Phosphorylation	TDEQALLSSILAKTA CHHHHHHHHHHHHHH	19.04	30266825
56	Phosphorylation	DEQALLSSILAKTAS HHHHHHHHHHHHHHH	22.91	19664994
60	Ubiquitination	LLSSILAKTASNIID HHHHHHHHHHHCCCC	40.97	33845483
61	Phosphorylation	LSSILAKTASNIIDV HHHHHHHHHHCCCCH	29.70	28450419
63	Phosphorylation	SILAKTASNIIDVSA HHHHHHHHCCCCHHH	33.52	23401153
69	Phosphorylation	ASNIIDVSAADSQGM HHCCCCHHHHHHCCC	17.62	28555341
73	Phosphorylation	IDVSAADSQGMEQHE CCHHHHHHCCCHHHH	24.73	23312004
81	Phosphorylation	QGMEQHEYMDRARQY CCCHHHHHHHHHHHH	11.37	23186163
96	Phosphorylation	STRLAVLSSSLTHWK HHHHHHHHHCCCCHH	15.98	30266825
97	Phosphorylation	TRLAVLSSSLTHWKK HHHHHHHHCCCCHHH	25.80	30266825
98	Phosphorylation	RLAVLSSSLTHWKKL HHHHHHHCCCCHHHC	33.63	22167270
100	Phosphorylation	AVLSSSLTHWKKLPP HHHHHCCCCHHHCCC	27.86	22167270
103	Ubiquitination	SSSLTHWKKLPPLPS HHCCCCHHHCCCCCC	36.51	33845483
103	2-Hydroxyisobutyrylation	SSSLTHWKKLPPLPS HHCCCCHHHCCCCCC	36.51	-
104	Ubiquitination	SSLTHWKKLPPLPSL HCCCCHHHCCCCCCC	62.12	22817900
110	Phosphorylation	KKLPPLPSLTSQPHQ HHCCCCCCCCCCCCE	52.54	26657352
112	Phosphorylation	LPPLPSLTSQPHQVL CCCCCCCCCCCCEEH	29.65	24173317
113	Phosphorylation	PPLPSLTSQPHQVLA CCCCCCCCCCCEEHH	47.19	28464451
121	Phosphorylation	QPHQVLASEPIPFSD CCCEEHHCCCCCHHH	39.48	24173317
127	Phosphorylation	ASEPIPFSDLQQVSR HCCCCCHHHHHHHHH	31.86	28122231
133	Phosphorylation	FSDLQQVSRIAAYAY HHHHHHHHHHHHHHH	17.40	28122231
138	Phosphorylation	QVSRIAAYAYSALSQ HHHHHHHHHHHHHHC	9.32	21945579
140	Phosphorylation	SRIAAYAYSALSQIR HHHHHHHHHHHHCCC	5.04	21945579
141	Phosphorylation	RIAAYAYSALSQIRV HHHHHHHHHHHCCCC	17.98	21945579
144	Phosphorylation	AYAYSALSQIRVDAK HHHHHHHHCCCCCCC	24.23	21945579

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LTOR1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CC90B_HUMAN	CCDC90B	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
LTOR2_HUMAN	LAMTOR2	physical	22939629
LTOR3_HUMAN	LAMTOR3	physical	22939629
GNAS3_HUMAN	GNAS	physical	22939629
GNAS2_HUMAN	GNAS	physical	22939629
ALEX_HUMAN	GNAS	physical	22939629
GNAS1_HUMAN	GNAS	physical	22939629
S2546_HUMAN	SLC25A46	physical	22939629
VATB1_HUMAN	ATP6V1B1	physical	22939629
LTOR5_HUMAN	LAMTOR5	physical	22980980
LTOR4_HUMAN	LAMTOR4	physical	22980980
RRAGB_HUMAN	RRAGB	physical	20381137
S38A9_HUMAN	SLC38A9	physical	25567906

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LTOR1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40, AND MASSSPECTROMETRY.	15592455 [Abstract]