Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2C74

14-3-3 Protein Eta (Human) Complexed to Peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0002028biological_processregulation of sodium ion transport
A0003779molecular_functionactin binding
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006713biological_processglucocorticoid catabolic process
A0006886biological_processintracellular protein transport
A0007165biological_processsignal transduction
A0008104biological_processprotein localization
A0014704cellular_componentintercalated disc
A0017080molecular_functionsodium channel regulator activity
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0021762biological_processsubstantia nigra development
A0035259molecular_functionnuclear glucocorticoid receptor binding
A0042802molecular_functionidentical protein binding
A0042921biological_processnuclear receptor-mediated glucocorticoid signaling pathway
A0044325molecular_functiontransmembrane transporter binding
A0045664biological_processregulation of neuron differentiation
A0045893biological_processpositive regulation of DNA-templated transcription
A0046982molecular_functionprotein heterodimerization activity
A0048167biological_processregulation of synaptic plasticity
A0050774biological_processnegative regulation of dendrite morphogenesis
A0070062cellular_componentextracellular exosome
A0086010biological_processmembrane depolarization during action potential
A0098793cellular_componentpresynapse
A0098978cellular_componentglutamatergic synapse
A0099171biological_processpresynaptic modulation of chemical synaptic transmission
A0150048cellular_componentcerebellar granule cell to Purkinje cell synapse
A2000649biological_processregulation of sodium ion transmembrane transporter activity
B0002028biological_processregulation of sodium ion transport
B0003779molecular_functionactin binding
B0005159molecular_functioninsulin-like growth factor receptor binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006713biological_processglucocorticoid catabolic process
B0006886biological_processintracellular protein transport
B0007165biological_processsignal transduction
B0008104biological_processprotein localization
B0014704cellular_componentintercalated disc
B0017080molecular_functionsodium channel regulator activity
B0019899molecular_functionenzyme binding
B0019904molecular_functionprotein domain specific binding
B0021762biological_processsubstantia nigra development
B0035259molecular_functionnuclear glucocorticoid receptor binding
B0042802molecular_functionidentical protein binding
B0042921biological_processnuclear receptor-mediated glucocorticoid signaling pathway
B0044325molecular_functiontransmembrane transporter binding
B0045664biological_processregulation of neuron differentiation
B0045893biological_processpositive regulation of DNA-templated transcription
B0046982molecular_functionprotein heterodimerization activity
B0048167biological_processregulation of synaptic plasticity
B0050774biological_processnegative regulation of dendrite morphogenesis
B0070062cellular_componentextracellular exosome
B0086010biological_processmembrane depolarization during action potential
B0098793cellular_componentpresynapse
B0098978cellular_componentglutamatergic synapse
B0099171biological_processpresynaptic modulation of chemical synaptic transmission
B0150048cellular_componentcerebellar granule cell to Purkinje cell synapse
B2000649biological_processregulation of sodium ion transmembrane transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CIT A 1237
ChainResidue
ALYS88
APHE115
AGLN116
ASER119
BARG10

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG42-VAL52

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR216-SER235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Interaction with phosphoserine on interacting protein
ChainResidueDetails
ASER58
ATYR133
BSER58
BTYR133

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylglycine => ECO:0000269|Ref.11
ChainResidueDetails
AASP3
BASP3

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
AALA26
BALA26

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68510
ChainResidueDetails
ATRP60
BTRP60

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon