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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
AA0005829cellular_componentcytosol
AA0005886cellular_componentplasma membrane
AA0006713biological_processglucocorticoid catabolic process
AA0006886biological_processintracellular protein transport
AA0007165biological_processsignal transduction
AA0008104biological_processprotein 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_processintracellular glucocorticoid receptor signaling pathway
AA0044325molecular_functiontransmembrane transporter binding
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
AA2000649biological_processregulation of sodium ion transmembrane transporter activity
BA0002028biological_processregulation of sodium ion transport
BA0003779molecular_functionactin binding
BA0005159molecular_functioninsulin-like growth factor receptor binding
BA0005515molecular_functionprotein binding
BA0005737cellular_componentcytoplasm
BA0005829cellular_componentcytosol
BA0005886cellular_componentplasma membrane
BA0006713biological_processglucocorticoid catabolic process
BA0006886biological_processintracellular protein transport
BA0007165biological_processsignal transduction
BA0008104biological_processprotein 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_processintracellular glucocorticoid receptor signaling pathway
BA0044325molecular_functiontransmembrane transporter binding
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
BA2000649biological_processregulation of sodium ion transmembrane transporter activity
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 Residues1
DetailsMOD_RES: Phosphoserine; by WNK1 and WNK4 => ECO:0000269|PubMed:15328345, ECO:0000269|PubMed:20525693, ECO:0007744|PubMed:18669648
ChainResidueDetails
AAARG134
CSEP342
BAARG59
BAARG134

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by SGK1 => ECO:0000305|PubMed:15328345
ChainResidueDetails
CALA367
BAGLY4

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
BASER27
CSER446

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA and SGK1 => ECO:0000269|PubMed:15328345, ECO:0000269|PubMed:15677482, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSEP448
BASER61

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by WNK1 and WNK4 => ECO:0000269|PubMed:20525693, ECO:0007744|PubMed:18669648
ChainResidueDetails
CSER449

221051

PDB entries from 2024-06-12

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