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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9R2N

Cryo-EM structure of the complex CCNY:14-3-3

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
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006713biological_processglucocorticoid catabolic process
A0006886biological_processintracellular protein transport
A0007165biological_processsignal transduction
A0008104biological_processintracellular protein 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
A0045202cellular_componentsynapse
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
B0002028biological_processregulation of sodium ion transport
B0003779molecular_functionactin binding
B0005159molecular_functioninsulin-like growth factor receptor binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006713biological_processglucocorticoid catabolic process
B0006886biological_processintracellular protein transport
B0007165biological_processsignal transduction
B0008104biological_processintracellular protein 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
B0045202cellular_componentsynapse
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
D0000086biological_processG2/M transition of mitotic cell cycle
D0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
D0000308cellular_componentcytoplasmic cyclin-dependent protein kinase holoenzyme complex
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005886cellular_componentplasma membrane
D0007283biological_processspermatogenesis
D0010508biological_processpositive regulation of autophagy
D0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
D0045737biological_processpositive regulation of cyclin-dependent protein serine/threonine kinase activity
D0060828biological_processregulation of canonical Wnt signaling pathway
D0061575molecular_functioncyclin-dependent protein serine/threonine kinase activator activity
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: {"description":"Interaction with phosphoserine on interacting protein"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
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 Residues122
DetailsDomain: {"description":"Cyclin N-terminal"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24794231","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BGU5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CDK14","evidences":[{"source":"PubMed","id":"24794231","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22184064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24794231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

256158

PDB entries from 2026-07-08

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