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2BR9

14-3-3 Protein Epsilon (Human) Complexed to 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
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
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
A0031625molecular_functionubiquitin protein ligase binding
A0031966cellular_componentmitochondrial membrane
A0034122biological_processnegative regulation of toll-like receptor signaling pathway
A0034504biological_processprotein localization to nucleus
A0034605biological_processcellular response to heat
A0035308biological_processnegative regulation of protein dephosphorylation
A0035332biological_processpositive regulation of hippo signaling
A0035556biological_processintracellular signal transduction
A0035591molecular_functionsignaling adaptor activity
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042826molecular_functionhistone deacetylase binding
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
A0051220biological_processcytoplasmic sequestering of protein
A0051480biological_processregulation of cytosolic calcium ion concentration
A0060306biological_processregulation of membrane repolarization
A0070062cellular_componentextracellular exosome
A0070972biological_processprotein localization to endoplasmic reticulum
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
A1901016biological_processregulation of potassium ion transmembrane transporter activity
A1902309biological_processnegative regulation of peptidyl-serine dephosphorylation
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

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR214-SER233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interaction with phosphoserine on interacting protein
ChainResidueDetails
AARG57
AARG130

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.13, ECO:0007744|PubMed:19413330
ChainResidueDetails
AMET1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS50

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62260
ChainResidueDetails
ASER65

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS69
ALYS118
ALYS123

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62260
ChainResidueDetails
ATYR131

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62260
ChainResidueDetails
ATHR137

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER210

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR232

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS50

219140

PDB entries from 2024-05-01

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