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6EIH

The crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0001764biological_processneuron migration
A0002753biological_processcytoplasmic pattern recognition receptor signaling pathway
A0003064biological_processregulation of heart rate by hormone
A0003723molecular_functionRNA binding
A0004864molecular_functionprotein phosphatase inhibitor activity
A0005246molecular_functioncalcium channel regulator activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006605biological_processprotein targeting
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0006893biological_processGolgi to plasma membrane transport
A0007165biological_processsignal transduction
A0007346biological_processregulation of mitotic cell cycle
A0008104biological_processprotein localization
A0015459molecular_functionpotassium channel regulator activity
A0016020cellular_componentmembrane
A0019855molecular_functioncalcium channel inhibitor activity
A0019899molecular_functionenzyme binding
A0019903molecular_functionprotein phosphatase binding
A0019904molecular_functionprotein domain specific binding
A0021762biological_processsubstantia nigra development
A0021766biological_processhippocampus development
A0021987biological_processcerebral cortex development
A0023026molecular_functionMHC class II protein complex binding
A0030007biological_processintracellular potassium ion homeostasis
A0031625molecular_functionubiquitin protein ligase binding
A0031966cellular_componentmitochondrial membrane
A0034122biological_processnegative regulation of toll-like receptor signaling pathway
A0034123biological_processpositive regulation of toll-like receptor signaling pathway
A0034142biological_processtoll-like receptor 4 signaling pathway
A0034504biological_processprotein localization to nucleus
A0034605biological_processcellular response to heat
A0035329biological_processhippo signaling
A0035332biological_processpositive regulation of hippo signaling
A0035556biological_processintracellular signal transduction
A0035591molecular_functionsignaling adaptor activity
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042826molecular_functionhistone deacetylase binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0044325molecular_functiontransmembrane transporter binding
A0045296molecular_functioncadherin binding
A0046827biological_processpositive regulation of protein export from nucleus
A0046982molecular_functionprotein heterodimerization activity
A0050815molecular_functionphosphoserine residue binding
A0051219molecular_functionphosphoprotein binding
A0051480biological_processregulation of cytosolic calcium ion concentration
A0060306biological_processregulation of membrane repolarization
A0070062cellular_componentextracellular exosome
A0070972biological_processprotein localization to endoplasmic reticulum
A0070979biological_processprotein K11-linked ubiquitination
A0086013biological_processmembrane repolarization during cardiac muscle cell action potential
A0086091biological_processregulation of heart rate by cardiac conduction
A0097110molecular_functionscaffold protein binding
A0140311molecular_functionprotein sequestering activity
A0140678molecular_functionmolecular function inhibitor activity
A1901379biological_processregulation of potassium ion transmembrane transport
A1905913biological_processnegative regulation of calcium ion export across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG42-VAL52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62260","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62260","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62260","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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