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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8DP5

Structure of the PEAK3/14-3-3 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005515molecular_functionprotein binding
A0005925cellular_componentfocal adhesion
A0008360biological_processregulation of cell shape
A0015629cellular_componentactin cytoskeleton
A0032956biological_processregulation of actin cytoskeleton organization
A2000145biological_processregulation of cell motility
B0004672molecular_functionprotein kinase activity
B0005515molecular_functionprotein binding
B0005925cellular_componentfocal adhesion
B0008360biological_processregulation of cell shape
B0015629cellular_componentactin cytoskeleton
B0032956biological_processregulation of actin cytoskeleton organization
B2000145biological_processregulation of cell motility
C0004860molecular_functionprotein kinase inhibitor activity
C0004864molecular_functionprotein phosphatase inhibitor activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005774cellular_componentvacuolar membrane
C0005829cellular_componentcytosol
C0005925cellular_componentfocal adhesion
C0007165biological_processsignal transduction
C0008104biological_processintracellular protein localization
C0016020cellular_componentmembrane
C0017053cellular_componenttranscription repressor complex
C0019899molecular_functionenzyme binding
C0019904molecular_functionprotein domain specific binding
C0032991cellular_componentprotein-containing complex
C0042308biological_processnegative regulation of protein import into nucleus
C0042470cellular_componentmelanosome
C0042802molecular_functionidentical protein binding
C0042826molecular_functionhistone deacetylase binding
C0044877molecular_functionprotein-containing complex binding
C0045296molecular_functioncadherin binding
C0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
C0045892biological_processnegative regulation of DNA-templated transcription
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0048471cellular_componentperinuclear region of cytoplasm
C0050815molecular_functionphosphoserine residue binding
C0051219molecular_functionphosphoprotein binding
C0070062cellular_componentextracellular exosome
C0140311molecular_functionprotein sequestering activity
D0000165biological_processMAPK cascade
D0002753biological_processcytoplasmic pattern recognition receptor signaling pathway
D0003064biological_processregulation of heart rate by hormone
D0003723molecular_functionRNA binding
D0004864molecular_functionprotein phosphatase inhibitor activity
D0005246molecular_functioncalcium channel regulator activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0007165biological_processsignal transduction
D0007346biological_processregulation of mitotic cell cycle
D0008104biological_processintracellular protein localization
D0015459molecular_functionpotassium channel regulator activity
D0016020cellular_componentmembrane
D0019855molecular_functioncalcium channel inhibitor activity
D0019899molecular_functionenzyme binding
D0019903molecular_functionprotein phosphatase binding
D0019904molecular_functionprotein domain specific binding
D0021762biological_processsubstantia nigra development
D0023026molecular_functionMHC class II protein complex binding
D0030007biological_processintracellular potassium ion homeostasis
D0031625molecular_functionubiquitin protein ligase binding
D0031966cellular_componentmitochondrial membrane
D0034122biological_processnegative regulation of toll-like receptor signaling pathway
D0034504biological_processprotein localization to nucleus
D0034605biological_processcellular response to heat
D0035332biological_processpositive regulation of hippo signaling
D0035556biological_processintracellular signal transduction
D0035591molecular_functionsignaling adaptor activity
D0042308biological_processnegative regulation of protein import into nucleus
D0042470cellular_componentmelanosome
D0042802molecular_functionidentical protein binding
D0042826molecular_functionhistone deacetylase binding
D0044325molecular_functiontransmembrane transporter binding
D0045296molecular_functioncadherin binding
D0046827biological_processpositive regulation of protein export from nucleus
D0046982molecular_functionprotein heterodimerization activity
D0050815molecular_functionphosphoserine residue binding
D0051219molecular_functionphosphoprotein binding
D0051480biological_processregulation of cytosolic calcium ion concentration
D0060306biological_processregulation of membrane repolarization
D0070062cellular_componentextracellular exosome
D0070972biological_processprotein localization to endoplasmic reticulum
D0086013biological_processmembrane repolarization during cardiac muscle cell action potential
D0086091biological_processregulation of heart rate by cardiac conduction
D0097110molecular_functionscaffold protein binding
D0140311molecular_functionprotein sequestering activity
D0140678molecular_functionmolecular function inhibitor activity
D1901379biological_processregulation of potassium ion transmembrane transport
D1905913biological_processnegative regulation of calcium ion export across plasma membrane
E0004672molecular_functionprotein kinase activity
E0005515molecular_functionprotein binding
E0005925cellular_componentfocal adhesion
E0008360biological_processregulation of cell shape
E0015629cellular_componentactin cytoskeleton
E0032956biological_processregulation of actin cytoskeleton organization
E2000145biological_processregulation of cell motility
P0004672molecular_functionprotein kinase activity
P0005515molecular_functionprotein binding
P0005925cellular_componentfocal adhesion
P0008360biological_processregulation of cell shape
P0015629cellular_componentactin cytoskeleton
P0032956biological_processregulation of actin cytoskeleton organization
P2000145biological_processregulation of cell motility
Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
DARG42-VAL52
CARG43-VAL53
site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
DTYR214-SER233
CTYR213-SER232
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues5
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68251","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","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":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62260","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62260","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62260","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
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_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
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

247536

PDB entries from 2026-01-14

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