9F43

cryo-EM structure of human LST2 bound to human mTOR complex 1, focused on RAPTOR

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0000045	biological_process	autophagosome assembly
E	0001558	biological_process	regulation of cell growth
E	0001938	biological_process	positive regulation of endothelial cell proliferation
E	0002181	biological_process	cytoplasmic translation
E	0005515	molecular_function	protein binding
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005764	cellular_component	lysosome
E	0005765	cellular_component	lysosomal membrane
E	0005829	cellular_component	cytosol
E	0006974	biological_process	DNA damage response
E	0008361	biological_process	regulation of cell size
E	0009267	biological_process	cellular response to starvation
E	0009410	biological_process	response to xenobiotic stimulus
E	0010494	cellular_component	cytoplasmic stress granule
E	0010506	biological_process	regulation of autophagy
E	0010507	biological_process	negative regulation of autophagy
E	0010646	biological_process	regulation of cell communication
E	0016020	cellular_component	membrane
E	0019901	molecular_function	protein kinase binding
E	0023051	biological_process	regulation of signaling
E	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
E	0030295	molecular_function	protein kinase activator activity
E	0030307	biological_process	positive regulation of cell growth
E	0030425	cellular_component	dendrite
E	0030674	molecular_function	protein-macromolecule adaptor activity
E	0031267	molecular_function	small GTPase binding
E	0031669	biological_process	cellular response to nutrient levels
E	0031929	biological_process	TOR signaling
E	0031931	cellular_component	TORC1 complex
E	0032008	biological_process	positive regulation of TOR signaling
E	0035176	biological_process	social behavior
E	0038202	biological_process	TORC1 signaling
E	0043025	cellular_component	neuronal cell body
E	0044877	molecular_function	protein-containing complex binding
E	0045672	biological_process	positive regulation of osteoclast differentiation
E	0045821	biological_process	positive regulation of glycolytic process
E	0045945	biological_process	positive regulation of transcription by RNA polymerase III
E	0045947	biological_process	negative regulation of translational initiation
E	0045948	biological_process	positive regulation of translational initiation
E	0046889	biological_process	positive regulation of lipid biosynthetic process
E	0061462	biological_process	protein localization to lysosome
E	0065008	biological_process	regulation of biological quality
E	0071230	biological_process	cellular response to amino acid stimulus
E	0071233	biological_process	cellular response to L-leucine
E	0071333	biological_process	cellular response to glucose stimulus
E	0071456	biological_process	cellular response to hypoxia
E	0071470	biological_process	cellular response to osmotic stress
E	0071889	molecular_function	14-3-3 protein binding
E	0140767	molecular_function	enzyme-substrate adaptor activity
E	1900087	biological_process	positive regulation of G1/S transition of mitotic cell cycle
E	1901331	biological_process	positive regulation of odontoblast differentiation
E	1902554	cellular_component	serine/threonine protein kinase complex
E	1904263	biological_process	positive regulation of TORC1 signaling
E	1905857	biological_process	positive regulation of pentose-phosphate shunt
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005768	cellular_component	endosome
G	0005829	cellular_component	cytosol
G	0007175	biological_process	negative regulation of epidermal growth factor-activated receptor activity
G	0008270	molecular_function	zinc ion binding
G	0016020	cellular_component	membrane
G	0031901	cellular_component	early endosome membrane
G	0032266	molecular_function	phosphatidylinositol-3-phosphate binding
G	0042059	biological_process	negative regulation of epidermal growth factor receptor signaling pathway
G	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	41
Details	Repeat: {"description":"WD 1"}

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site_id	SWS_FT_FI2
Number of Residues	41
Details	Repeat: {"description":"WD 2"}

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site_id	SWS_FT_FI3
Number of Residues	39
Details	Repeat: {"description":"WD 4"}

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site_id	SWS_FT_FI4
Number of Residues	40
Details	Repeat: {"description":"WD 5"}

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site_id	SWS_FT_FI5
Number of Residues	40
Details	Repeat: {"description":"WD 6"}

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site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"31530866","evidenceCode":"ECO:0000269"}]}

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site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"30197302","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32561715","evidenceCode":"ECO:0000269"}]}

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