Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7NMZ

Structure of 14-3-3 eta in complex with Nedd4-2(335-455) containing two 14-3-3 binding motifs Ser342 and Ser448

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AA0002028biological_processregulation of sodium ion transport
AA0003779molecular_functionactin binding
AA0005159molecular_functioninsulin-like growth factor receptor binding
AA0005515molecular_functionprotein binding
AA0005737cellular_componentcytoplasm
AA0005739cellular_componentmitochondrion
AA0005829cellular_componentcytosol
AA0005886cellular_componentplasma membrane
AA0006713biological_processglucocorticoid catabolic process
AA0006886biological_processintracellular protein transport
AA0007165biological_processsignal transduction
AA0008104biological_processintracellular protein localization
AA0014704cellular_componentintercalated disc
AA0017080molecular_functionsodium channel regulator activity
AA0019899molecular_functionenzyme binding
AA0019904molecular_functionprotein domain specific binding
AA0021762biological_processsubstantia nigra development
AA0035259molecular_functionnuclear glucocorticoid receptor binding
AA0042802molecular_functionidentical protein binding
AA0042921biological_processnuclear receptor-mediated glucocorticoid signaling pathway
AA0044325molecular_functiontransmembrane transporter binding
AA0045202cellular_componentsynapse
AA0045664biological_processregulation of neuron differentiation
AA0045893biological_processpositive regulation of DNA-templated transcription
AA0046982molecular_functionprotein heterodimerization activity
AA0048167biological_processregulation of synaptic plasticity
AA0050774biological_processnegative regulation of dendrite morphogenesis
AA0070062cellular_componentextracellular exosome
AA0086010biological_processmembrane depolarization during action potential
AA0098793cellular_componentpresynapse
AA0098978cellular_componentglutamatergic synapse
AA0099171biological_processpresynaptic modulation of chemical synaptic transmission
AA0150048cellular_componentcerebellar granule cell to Purkinje cell synapse
BA0002028biological_processregulation of sodium ion transport
BA0003779molecular_functionactin binding
BA0005159molecular_functioninsulin-like growth factor receptor binding
BA0005515molecular_functionprotein binding
BA0005737cellular_componentcytoplasm
BA0005739cellular_componentmitochondrion
BA0005829cellular_componentcytosol
BA0005886cellular_componentplasma membrane
BA0006713biological_processglucocorticoid catabolic process
BA0006886biological_processintracellular protein transport
BA0007165biological_processsignal transduction
BA0008104biological_processintracellular protein localization
BA0014704cellular_componentintercalated disc
BA0017080molecular_functionsodium channel regulator activity
BA0019899molecular_functionenzyme binding
BA0019904molecular_functionprotein domain specific binding
BA0021762biological_processsubstantia nigra development
BA0035259molecular_functionnuclear glucocorticoid receptor binding
BA0042802molecular_functionidentical protein binding
BA0042921biological_processnuclear receptor-mediated glucocorticoid signaling pathway
BA0044325molecular_functiontransmembrane transporter binding
BA0045202cellular_componentsynapse
BA0045664biological_processregulation of neuron differentiation
BA0045893biological_processpositive regulation of DNA-templated transcription
BA0046982molecular_functionprotein heterodimerization activity
BA0048167biological_processregulation of synaptic plasticity
BA0050774biological_processnegative regulation of dendrite morphogenesis
BA0070062cellular_componentextracellular exosome
BA0086010biological_processmembrane depolarization during action potential
BA0098793cellular_componentpresynapse
BA0098978cellular_componentglutamatergic synapse
BA0099171biological_processpresynaptic modulation of chemical synaptic transmission
BA0150048cellular_componentcerebellar granule cell to Purkinje cell synapse
Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AAARG44-VAL54
site_idPS01159
Number of Residues26
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. Weerkdakgrt.YYvnhnnrtTTWTRP
ChainResidueDetails
CTRP391-PRO416
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylglycine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68510","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by WNK1 and WNK4","evidences":[{"source":"PubMed","id":"15328345","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20525693","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA and SGK1","evidences":[{"source":"PubMed","id":"15328345","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15677482","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by WNK1 and WNK4","evidences":[{"source":"PubMed","id":"20525693","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

PDB statisticsPDBj update infoContact PDBjnumon