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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6SAD

Structure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on Ser139 and Ser164

Functional Information from GO Data
ChainGOidnamespacecontents
A0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
A0003723molecular_functionRNA binding
A0005080molecular_functionprotein kinase C binding
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006469biological_processnegative regulation of protein kinase activity
A0006605biological_processprotein targeting
A0007165biological_processsignal transduction
A0008104biological_processintracellular protein localization
A0008426molecular_functionprotein kinase C inhibitor activity
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0019904molecular_functionprotein domain specific binding
A0022409biological_processpositive regulation of cell-cell adhesion
A0030971molecular_functionreceptor tyrosine kinase binding
A0031982cellular_componentvesicle
A0032869biological_processcellular response to insulin stimulus
A0032880biological_processregulation of protein localization
A0042149biological_processcellular response to glucose starvation
A0042802molecular_functionidentical protein binding
A0045202cellular_componentsynapse
A0045664biological_processregulation of neuron differentiation
A0048167biological_processregulation of synaptic plasticity
A0050870biological_processpositive regulation of T cell activation
A0070062cellular_componentextracellular exosome
A0098793cellular_componentpresynapse
A0140031molecular_functionphosphorylation-dependent protein binding
A0140311molecular_functionprotein sequestering activity
A1904262biological_processnegative regulation of TORC1 signaling
B0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
B0003723molecular_functionRNA binding
B0005080molecular_functionprotein kinase C binding
B0005159molecular_functioninsulin-like growth factor receptor binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006469biological_processnegative regulation of protein kinase activity
B0006605biological_processprotein targeting
B0007165biological_processsignal transduction
B0008104biological_processintracellular protein localization
B0008426molecular_functionprotein kinase C inhibitor activity
B0009966biological_processregulation of signal transduction
B0016020cellular_componentmembrane
B0019904molecular_functionprotein domain specific binding
B0022409biological_processpositive regulation of cell-cell adhesion
B0030971molecular_functionreceptor tyrosine kinase binding
B0031982cellular_componentvesicle
B0032869biological_processcellular response to insulin stimulus
B0032880biological_processregulation of protein localization
B0042149biological_processcellular response to glucose starvation
B0042802molecular_functionidentical protein binding
B0045202cellular_componentsynapse
B0045664biological_processregulation of neuron differentiation
B0048167biological_processregulation of synaptic plasticity
B0050870biological_processpositive regulation of T cell activation
B0070062cellular_componentextracellular exosome
B0098793cellular_componentpresynapse
B0140031molecular_functionphosphorylation-dependent protein binding
B0140311molecular_functionprotein sequestering activity
B1904262biological_processnegative regulation of TORC1 signaling
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 Residues328
DetailsRegion: {"description":"Required for interaction with SPATA18/MIEAP (isoform 2) but dispensable for binding to SPATA18/MIEAP (isoform 1)","evidences":[{"source":"PubMed","id":"22532927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"source":"PubMed","id":"17085597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N-acetylvaline; partial","evidences":[{"source":"PubMed","id":"14534293","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P61983","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P61983","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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