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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9NIE

Cryo-EM structure of the PI3K alpha/KRas/HER3 phosphopeptide complex on POPC/POPS/PIP2 nanodiscs low-pass filtered to 5 angstroms

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0001944biological_processvasculature development
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005942cellular_componentphosphatidylinositol 3-kinase complex
A0005943cellular_componentphosphatidylinositol 3-kinase complex, class IA
A0005944cellular_componentphosphatidylinositol 3-kinase complex, class IB
A0007173biological_processepidermal growth factor receptor signaling pathway
A0008286biological_processinsulin receptor signaling pathway
A0010592biological_processpositive regulation of lamellipodium assembly
A0010629biological_processnegative regulation of gene expression
A0014704cellular_componentintercalated disc
A0014823biological_processresponse to activity
A0014870biological_processresponse to muscle inactivity
A0016242biological_processnegative regulation of macroautophagy
A0016303molecular_function1-phosphatidylinositol-3-kinase activity
A0016477biological_processcell migration
A0030027cellular_componentlamellipodium
A0030036biological_processactin cytoskeleton organization
A0030168biological_processplatelet activation
A0030295molecular_functionprotein kinase activator activity
A0030593biological_processneutrophil chemotaxis
A0030835biological_processnegative regulation of actin filament depolymerization
A0032008biological_processpositive regulation of TOR signaling
A0032869biological_processcellular response to insulin stimulus
A0035005molecular_function1-phosphatidylinositol-4-phosphate 3-kinase activity
A0035994biological_processresponse to muscle stretch
A0036092biological_processphosphatidylinositol-3-phosphate biosynthetic process
A0038084biological_processvascular endothelial growth factor signaling pathway
A0038112biological_processinterleukin-8-mediated signaling pathway
A0038203biological_processTORC2 signaling
A0043201biological_processresponse to L-leucine
A0043276biological_processanoikis
A0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
A0043542biological_processendothelial cell migration
A0043560molecular_functioninsulin receptor substrate binding
A0045860biological_processpositive regulation of protein kinase activity
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0046934molecular_function1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity
A0048009biological_processinsulin-like growth factor receptor signaling pathway
A0048015biological_processphosphatidylinositol-mediated signaling
A0048471cellular_componentperinuclear region of cytoplasm
A0048661biological_processpositive regulation of smooth muscle cell proliferation
A0050852biological_processT cell receptor signaling pathway
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0055119biological_processrelaxation of cardiac muscle
A0060048biological_processcardiac muscle contraction
A0071464biological_processcellular response to hydrostatic pressure
A0071548biological_processresponse to dexamethasone
A0086003biological_processcardiac muscle cell contraction
A0106310molecular_functionprotein serine kinase activity
A0110053biological_processregulation of actin filament organization
A1903544biological_processresponse to butyrate
A1905477biological_processpositive regulation of protein localization to membrane
A2000811biological_processnegative regulation of anoikis
C0000139cellular_componentGolgi membrane
C0000164cellular_componentprotein phosphatase type 1 complex
C0000165biological_processMAPK cascade
C0001889biological_processliver development
C0003924molecular_functionGTPase activity
C0003925molecular_functionG protein activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005741cellular_componentmitochondrial outer membrane
C0005789cellular_componentendoplasmic reticulum membrane
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0007249biological_processcanonical NF-kappaB signal transduction
C0007265biological_processRas protein signal transduction
C0007565biological_processfemale pregnancy
C0008284biological_processpositive regulation of cell population proliferation
C0009629biological_processresponse to gravity
C0009898cellular_componentcytoplasmic side of plasma membrane
C0010628biological_processpositive regulation of gene expression
C0012505cellular_componentendomembrane system
C0016020cellular_componentmembrane
C0019002molecular_functionGMP binding
C0019003molecular_functionGDP binding
C0019221biological_processcytokine-mediated signaling pathway
C0030275molecular_functionLRR domain binding
C0032008biological_processpositive regulation of TOR signaling
C0035900biological_processresponse to isolation stress
C0042127biological_processregulation of cell population proliferation
C0043069biological_processnegative regulation of programmed cell death
C0043410biological_processpositive regulation of MAPK cascade
C0044877molecular_functionprotein-containing complex binding
C0046579biological_processpositive regulation of Ras protein signal transduction
C0051384biological_processresponse to glucocorticoid
C0051385biological_processresponse to mineralocorticoid
C0051450biological_processmyoblast proliferation
C0060038biological_processcardiac muscle cell proliferation
C1902554cellular_componentserine/threonine protein kinase complex
C1905360cellular_componentGTPase complex
C2000774biological_processpositive regulation of cellular senescence
Functional Information from PROSITE/UniProt
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKng.DDLRQDmltlQ
ChainResidueDetails
APHE801-GLN815
site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycVatFILgIgDRHnsN
ChainResidueDetails
ASER900-ASN920
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues102
DetailsDomain: {"description":"PI3K-RBD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00879","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues286
DetailsDomain: {"description":"PI3K/PI4K catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues26
DetailsRegion: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Implicated in the recognition of ATP as well as PIP2. Also crucial for autophosphorylation of the p85alpha subunit","evidences":[{"source":"PubMed","id":"23936502","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsMotif: {"description":"Effector region"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22431598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22566140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34380736","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"40934300","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"9MF0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"40934300","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9MF0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine; in GTPase KRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"30442762","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

255615

PDB entries from 2026-06-24

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