Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9GCP

ChREBP/14-3-3 complex stabilized by AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004860molecular_functionprotein kinase inhibitor activity
A0004864molecular_functionprotein phosphatase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005774cellular_componentvacuolar membrane
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006605biological_processprotein targeting
A0007165biological_processsignal transduction
A0008104biological_processintracellular protein localization
A0016020cellular_componentmembrane
A0017053cellular_componenttranscription repressor complex
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0032991cellular_componentprotein-containing complex
A0035332biological_processpositive regulation of hippo signaling
A0042308biological_processnegative regulation of protein import into nucleus
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042826molecular_functionhistone deacetylase binding
A0044877molecular_functionprotein-containing complex binding
A0045296molecular_functioncadherin binding
A0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
A0045892biological_processnegative regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0048471cellular_componentperinuclear region of cytoplasm
A0050815molecular_functionphosphoserine residue binding
A0051219molecular_functionphosphoprotein binding
A0060243biological_processnegative regulation of cell growth involved in contact inhibition
A0070062cellular_componentextracellular exosome
A0140311molecular_functionprotein sequestering activity
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
C0006605biological_processprotein targeting
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
C0035332biological_processpositive regulation of hippo signaling
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
C0060243biological_processnegative regulation of cell growth involved in contact inhibition
C0070062cellular_componentextracellular exosome
C0140311molecular_functionprotein sequestering activity
E0004860molecular_functionprotein kinase inhibitor activity
E0004864molecular_functionprotein phosphatase inhibitor activity
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005774cellular_componentvacuolar membrane
E0005829cellular_componentcytosol
E0005925cellular_componentfocal adhesion
E0006605biological_processprotein targeting
E0007165biological_processsignal transduction
E0008104biological_processintracellular protein localization
E0016020cellular_componentmembrane
E0017053cellular_componenttranscription repressor complex
E0019899molecular_functionenzyme binding
E0019904molecular_functionprotein domain specific binding
E0032991cellular_componentprotein-containing complex
E0035332biological_processpositive regulation of hippo signaling
E0042308biological_processnegative regulation of protein import into nucleus
E0042470cellular_componentmelanosome
E0042802molecular_functionidentical protein binding
E0042826molecular_functionhistone deacetylase binding
E0044877molecular_functionprotein-containing complex binding
E0045296molecular_functioncadherin binding
E0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
E0045892biological_processnegative regulation of DNA-templated transcription
E0045944biological_processpositive regulation of transcription by RNA polymerase II
E0048471cellular_componentperinuclear region of cytoplasm
E0050815molecular_functionphosphoserine residue binding
E0051219molecular_functionphosphoprotein binding
E0060243biological_processnegative regulation of cell growth involved in contact inhibition
E0070062cellular_componentextracellular exosome
E0140311molecular_functionprotein sequestering activity
G0004860molecular_functionprotein kinase inhibitor activity
G0004864molecular_functionprotein phosphatase inhibitor activity
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005774cellular_componentvacuolar membrane
G0005829cellular_componentcytosol
G0005925cellular_componentfocal adhesion
G0006605biological_processprotein targeting
G0007165biological_processsignal transduction
G0008104biological_processintracellular protein localization
G0016020cellular_componentmembrane
G0017053cellular_componenttranscription repressor complex
G0019899molecular_functionenzyme binding
G0019904molecular_functionprotein domain specific binding
G0032991cellular_componentprotein-containing complex
G0035332biological_processpositive regulation of hippo signaling
G0042308biological_processnegative regulation of protein import into nucleus
G0042470cellular_componentmelanosome
G0042802molecular_functionidentical protein binding
G0042826molecular_functionhistone deacetylase binding
G0044877molecular_functionprotein-containing complex binding
G0045296molecular_functioncadherin binding
G0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
G0045892biological_processnegative regulation of DNA-templated transcription
G0045944biological_processpositive regulation of transcription by RNA polymerase II
G0048471cellular_componentperinuclear region of cytoplasm
G0050815molecular_functionphosphoserine residue binding
G0051219molecular_functionphosphoprotein binding
G0060243biological_processnegative regulation of cell growth involved in contact inhibition
G0070062cellular_componentextracellular exosome
G0140311molecular_functionprotein sequestering activity
Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG43-VAL53

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR213-SER232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68251","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
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_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

PDB statisticsPDBj update infoContact PDBjnumon