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6Y6B

Crystal structure of human 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser100 and 16-OMe-Fusicoccin H

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
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006469biological_processnegative regulation of protein kinase activity
A0006605biological_processprotein targeting
A0007165biological_processsignal transduction
A0008104biological_processprotein 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
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006469biological_processnegative regulation of protein kinase activity
B0006605biological_processprotein targeting
B0007165biological_processsignal transduction
B0008104biological_processprotein 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 PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue OD8 B 301
ChainResidue
BASN43
BVAL47
BPHE122
BLYS125
BMET126
BPRO170
BASP218
DGLU103

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
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8C078
ChainResidueDetails
CSEP100
DSEP100
BARG57
BARG132

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial => ECO:0000269|Ref.7
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylvaline; partial => ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330
ChainResidueDetails
AVAL2
BVAL2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER71
BSER71

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P61983
ChainResidueDetails
ATYR133
BTYR133

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|Ref.7
ChainResidueDetails
ATHR145
BTHR145

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P61983
ChainResidueDetails
ASER215
BSER215

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR234
BTHR234

223166

PDB entries from 2024-07-31

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