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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8RCK

CryoEM structure of mTORC1 with a paediatric kidney cancer-associated 1455-EWED-1458 duplication in mTOR, Focused on one protomer copy.

Functional Information from GO Data
ChainGOidnamespacecontents
B0000139cellular_componentGolgi membrane
B0000166molecular_functionnucleotide binding
B0000822molecular_functioninositol hexakisphosphate binding
B0001002molecular_functionRNA polymerase III type 1 promoter sequence-specific DNA binding
B0001003molecular_functionRNA polymerase III type 2 promoter sequence-specific DNA binding
B0001006molecular_functionRNA polymerase III type 3 promoter sequence-specific DNA binding
B0001156molecular_functionTFIIIC-class transcription factor complex binding
B0001558biological_processregulation of cell growth
B0002296biological_processT-helper 1 cell lineage commitment
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005741cellular_componentmitochondrial outer membrane
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006468biological_processprotein phosphorylation
B0006954biological_processinflammatory response
B0006974biological_processDNA damage response
B0007010biological_processcytoskeleton organization
B0008361biological_processregulation of cell size
B0009267biological_processcellular response to starvation
B0009408biological_processresponse to heat
B0009891biological_processpositive regulation of biosynthetic process
B0010506biological_processregulation of autophagy
B0010507biological_processnegative regulation of autophagy
B0010718biological_processpositive regulation of epithelial to mesenchymal transition
B0012505cellular_componentendomembrane system
B0016020cellular_componentmembrane
B0016241biological_processregulation of macroautophagy
B0016242biological_processnegative regulation of macroautophagy
B0016301molecular_functionkinase activity
B0016605cellular_componentPML body
B0016740molecular_functiontransferase activity
B0019216biological_processregulation of lipid metabolic process
B0019228biological_processneuronal action potential
B0030307biological_processpositive regulation of cell growth
B0030425cellular_componentdendrite
B0031295biological_processT cell costimulation
B0031410cellular_componentcytoplasmic vesicle
B0031667biological_processresponse to nutrient levels
B0031669biological_processcellular response to nutrient levels
B0031670biological_processcellular response to nutrient
B0031929biological_processTOR signaling
B0031931cellular_componentTORC1 complex
B0031932cellular_componentTORC2 complex
B0032869biological_processcellular response to insulin stimulus
B0032956biological_processregulation of actin cytoskeleton organization
B0034198biological_processcellular response to amino acid starvation
B0038202biological_processTORC1 signaling
B0038203biological_processTORC2 signaling
B0042752biological_processregulation of circadian rhythm
B0042802molecular_functionidentical protein binding
B0043022molecular_functionribosome binding
B0043066biological_processnegative regulation of apoptotic process
B0043200biological_processresponse to amino acid
B0043276biological_processanoikis
B0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
B0044325molecular_functiontransmembrane transporter binding
B0044877molecular_functionprotein-containing complex binding
B0045335cellular_componentphagocytic vesicle
B0045597biological_processpositive regulation of cell differentiation
B0045670biological_processregulation of osteoclast differentiation
B0045727biological_processpositive regulation of translation
B0045821biological_processpositive regulation of glycolytic process
B0045860biological_processpositive regulation of protein kinase activity
B0045945biological_processpositive regulation of transcription by RNA polymerase III
B0045948biological_processpositive regulation of translational initiation
B0046627biological_processnegative regulation of insulin receptor signaling pathway
B0046889biological_processpositive regulation of lipid biosynthetic process
B0048266biological_processbehavioral response to pain
B0050821biological_processprotein stabilization
B0051219molecular_functionphosphoprotein binding
B0051240biological_processpositive regulation of multicellular organismal process
B0051549biological_processpositive regulation of keratinocyte migration
B0051896biological_processregulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0055006biological_processcardiac cell development
B0061431biological_processcellular response to methionine
B0062027biological_processpositive regulation of SCF-dependent proteasomal ubiquitin-dependent catabolic process
B0071230biological_processcellular response to amino acid stimulus
B0071233biological_processcellular response to L-leucine
B0071456biological_processcellular response to hypoxia
B0071470biological_processcellular response to osmotic stress
B0080135biological_processregulation of cellular response to stress
B0097700biological_processvascular endothelial cell response to laminar fluid shear stress
B0106310molecular_functionprotein serine kinase activity
B1900034biological_processregulation of cellular response to heat
B1900181biological_processnegative regulation of protein localization to nucleus
B1901796biological_processregulation of signal transduction by p53 class mediator
B1901838biological_processpositive regulation of transcription of nucleolar large rRNA by RNA polymerase I
B1903691biological_processpositive regulation of wound healing, spreading of epidermal cells
B1904059biological_processregulation of locomotor rhythm
B1904690biological_processpositive regulation of cytoplasmic translational initiation
B1905671biological_processregulation of lysosome organization
B1905672biological_processnegative regulation of lysosome organization
B1905857biological_processpositive regulation of pentose-phosphate shunt
B1990253biological_processcellular response to leucine starvation
B2000060biological_processpositive regulation of ubiquitin-dependent protein catabolic process
B2000785biological_processregulation of autophagosome assembly
E0004674molecular_functionprotein serine/threonine kinase activity
E0005515molecular_functionprotein binding
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005765cellular_componentlysosomal membrane
E0005829cellular_componentcytosol
E0006974biological_processDNA damage response
E0007010biological_processcytoskeleton organization
E0010507biological_processnegative regulation of autophagy
E0030307biological_processpositive regulation of cell growth
E0030674molecular_functionprotein-macromolecule adaptor activity
E0031669biological_processcellular response to nutrient levels
E0031929biological_processTOR signaling
E0031931cellular_componentTORC1 complex
E0031932cellular_componentTORC2 complex
E0032008biological_processpositive regulation of TOR signaling
E0032956biological_processregulation of actin cytoskeleton organization
E0038202biological_processTORC1 signaling
E0038203biological_processTORC2 signaling
E0043066biological_processnegative regulation of apoptotic process
E0043539molecular_functionprotein serine/threonine kinase activator activity
E0045821biological_processpositive regulation of glycolytic process
E0046889biological_processpositive regulation of lipid biosynthetic process
E0071456biological_processcellular response to hypoxia
E0071470biological_processcellular response to osmotic stress
E1905857biological_processpositive regulation of pentose-phosphate shunt
X0000082biological_processG1/S transition of mitotic cell cycle
X0005515molecular_functionprotein binding
X0005634cellular_componentnucleus
X0005654cellular_componentnucleoplasm
X0005737cellular_componentcytoplasm
X0005829cellular_componentcytosol
X0006417biological_processregulation of translation
X0008190molecular_functioneukaryotic initiation factor 4E binding
X0017148biological_processnegative regulation of translation
X0030371molecular_functiontranslation repressor activity
X0031369molecular_functiontranslation initiation factor binding
X0031929biological_processTOR signaling
X0045931biological_processpositive regulation of mitotic cell cycle
X0045947biological_processnegative regulation of translational initiation
Y0001558biological_processregulation of cell growth
Y0001938biological_processpositive regulation of endothelial cell proliferation
Y0004674molecular_functionprotein serine/threonine kinase activity
Y0005515molecular_functionprotein binding
Y0005654cellular_componentnucleoplasm
Y0005737cellular_componentcytoplasm
Y0005764cellular_componentlysosome
Y0005765cellular_componentlysosomal membrane
Y0005829cellular_componentcytosol
Y0006974biological_processDNA damage response
Y0008361biological_processregulation of cell size
Y0009267biological_processcellular response to starvation
Y0009410biological_processresponse to xenobiotic stimulus
Y0010494cellular_componentcytoplasmic stress granule
Y0010506biological_processregulation of autophagy
Y0010507biological_processnegative regulation of autophagy
Y0010646biological_processregulation of cell communication
Y0019901molecular_functionprotein kinase binding
Y0023051biological_processregulation of signaling
Y0030291molecular_functionprotein serine/threonine kinase inhibitor activity
Y0030295molecular_functionprotein kinase activator activity
Y0030307biological_processpositive regulation of cell growth
Y0030425cellular_componentdendrite
Y0030674molecular_functionprotein-macromolecule adaptor activity
Y0031267molecular_functionsmall GTPase binding
Y0031669biological_processcellular response to nutrient levels
Y0031929biological_processTOR signaling
Y0031931cellular_componentTORC1 complex
Y0032008biological_processpositive regulation of TOR signaling
Y0035176biological_processsocial behavior
Y0038202biological_processTORC1 signaling
Y0043025cellular_componentneuronal cell body
Y0044877molecular_functionprotein-containing complex binding
Y0045672biological_processpositive regulation of osteoclast differentiation
Y0045821biological_processpositive regulation of glycolytic process
Y0045945biological_processpositive regulation of transcription by RNA polymerase III
Y0046889biological_processpositive regulation of lipid biosynthetic process
Y0060255biological_processregulation of macromolecule metabolic process
Y0071230biological_processcellular response to amino acid stimulus
Y0071233biological_processcellular response to L-leucine
Y0071333biological_processcellular response to glucose stimulus
Y0071456biological_processcellular response to hypoxia
Y0071470biological_processcellular response to osmotic stress
Y0071889molecular_function14-3-3 protein binding
Y0080090biological_processregulation of primary metabolic process
Y0140767molecular_functionenzyme-substrate adaptor activity
Y1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
Y1901331biological_processpositive regulation of odontoblast differentiation
Y1905857biological_processpositive regulation of pentose-phosphate shunt
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. MYTGgeDcTARIWDL
ChainResidueDetails
EMET100-LEU114
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. LKgh.EDLRQDervmQ
ChainResidueDetails
BLEU2186-GLN2200
site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. SlAvmsMvgYILgLgDRHpsN
ChainResidueDetails
BSER2323-ASN2343
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues37
DetailsRepeat: {"description":"HEAT 3"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues40
DetailsRepeat: {"description":"HEAT 5"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues38
DetailsRepeat: {"description":"HEAT 17"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues39
DetailsRepeat: {"description":"HEAT 18"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues39
DetailsRepeat: {"description":"HEAT 20"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues36
DetailsRepeat: {"description":"HEAT 21"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues45
DetailsRepeat: {"description":"HEAT 23"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues38
DetailsRepeat: {"description":"HEAT 24"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues39
DetailsRepeat: {"description":"HEAT 25"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues36
DetailsRepeat: {"description":"HEAT 26"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues38
DetailsRepeat: {"description":"HEAT 27"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues43
DetailsRepeat: {"description":"HEAT 28"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues37
DetailsRepeat: {"description":"HEAT 31"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues33
DetailsRepeat: {"description":"HEAT 32"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues36
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues25
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues39
DetailsRepeat: {"description":"TPR 8"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues34
DetailsRepeat: {"description":"TPR 9"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues43
DetailsRepeat: {"description":"TPR 10"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues37
DetailsRepeat: {"description":"TPR 11"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues54
DetailsRepeat: {"description":"TPR 12"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues32
DetailsRepeat: {"description":"TPR 14"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues39
DetailsRepeat: {"description":"TPR 15"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues34
DetailsRepeat: {"description":"TPR 16"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues32
DetailsDomain: {"description":"FATC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00534","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00535","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues132
DetailsRegion: {"description":"Sufficient for interaction with the FKBP1A/rapamycin complex","evidences":[{"source":"UniProtKB","id":"Q9JLN9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues6
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues38
DetailsRegion: {"description":"Interaction with MLST8"}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues8
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues25
DetailsRegion: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"33158864","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ZWM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19487463","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by TBK1","evidences":[{"source":"PubMed","id":"21576368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29150432","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21576368","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"24247430","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"37979583","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues40
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues39
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues39
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues39
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues39
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues41
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI47
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"34741373","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI48
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)","evidences":[{"source":"PubMed","id":"38395307","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI49
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"28489822","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI50
Number of Residues41
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI51
Number of Residues41
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI52
Number of Residues39
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI53
Number of Residues40
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI54
Number of Residues40
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI55
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"31530866","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI56
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"30197302","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32561715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI57
Number of Residues4
DetailsMotif: {"description":"TOS motif","evidences":[{"source":"PubMed","id":"12747827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24403073","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI58
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12588975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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