5D3E

Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002842	biological_process	positive regulation of T cell mediated immune response to tumor cell
A	0003723	molecular_function	RNA binding
A	0005080	molecular_function	protein kinase C binding
A	0005159	molecular_function	insulin-like growth factor receptor binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0005925	cellular_component	focal adhesion
A	0006469	biological_process	negative regulation of protein kinase activity
A	0006605	biological_process	protein targeting
A	0007165	biological_process	signal transduction
A	0008104	biological_process	intracellular protein localization
A	0008426	molecular_function	protein kinase C inhibitor activity
A	0009966	biological_process	regulation of signal transduction
A	0016020	cellular_component	membrane
A	0019904	molecular_function	protein domain specific binding
A	0022409	biological_process	positive regulation of cell-cell adhesion
A	0030971	molecular_function	receptor tyrosine kinase binding
A	0031982	cellular_component	vesicle
A	0032869	biological_process	cellular response to insulin stimulus
A	0032880	biological_process	regulation of protein localization
A	0042149	biological_process	cellular response to glucose starvation
A	0042802	molecular_function	identical protein binding
A	0045202	cellular_component	synapse
A	0045664	biological_process	regulation of neuron differentiation
A	0048167	biological_process	regulation of synaptic plasticity
A	0050870	biological_process	positive regulation of T cell activation
A	0070062	cellular_component	extracellular exosome
A	0098793	cellular_component	presynapse
A	0140031	molecular_function	phosphorylation-dependent protein binding
A	0140311	molecular_function	protein sequestering activity
A	1904262	biological_process	negative regulation of TORC1 signaling
B	0002842	biological_process	positive regulation of T cell mediated immune response to tumor cell
B	0003723	molecular_function	RNA binding
B	0005080	molecular_function	protein kinase C binding
B	0005159	molecular_function	insulin-like growth factor receptor binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005759	cellular_component	mitochondrial matrix
B	0005829	cellular_component	cytosol
B	0005925	cellular_component	focal adhesion
B	0006469	biological_process	negative regulation of protein kinase activity
B	0006605	biological_process	protein targeting
B	0007165	biological_process	signal transduction
B	0008104	biological_process	intracellular protein localization
B	0008426	molecular_function	protein kinase C inhibitor activity
B	0009966	biological_process	regulation of signal transduction
B	0016020	cellular_component	membrane
B	0019904	molecular_function	protein domain specific binding
B	0022409	biological_process	positive regulation of cell-cell adhesion
B	0030971	molecular_function	receptor tyrosine kinase binding
B	0031982	cellular_component	vesicle
B	0032869	biological_process	cellular response to insulin stimulus
B	0032880	biological_process	regulation of protein localization
B	0042149	biological_process	cellular response to glucose starvation
B	0042802	molecular_function	identical protein binding
B	0045202	cellular_component	synapse
B	0045664	biological_process	regulation of neuron differentiation
B	0048167	biological_process	regulation of synaptic plasticity
B	0050870	biological_process	positive regulation of T cell activation
B	0070062	cellular_component	extracellular exosome
B	0098793	cellular_component	presynapse
B	0140031	molecular_function	phosphorylation-dependent protein binding
B	0140311	molecular_function	protein sequestering activity
B	1904262	biological_process	negative regulation of TORC1 signaling
E	0002842	biological_process	positive regulation of T cell mediated immune response to tumor cell
E	0003723	molecular_function	RNA binding
E	0005080	molecular_function	protein kinase C binding
E	0005159	molecular_function	insulin-like growth factor receptor binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005759	cellular_component	mitochondrial matrix
E	0005829	cellular_component	cytosol
E	0005925	cellular_component	focal adhesion
E	0006469	biological_process	negative regulation of protein kinase activity
E	0006605	biological_process	protein targeting
E	0007165	biological_process	signal transduction
E	0008104	biological_process	intracellular protein localization
E	0008426	molecular_function	protein kinase C inhibitor activity
E	0009966	biological_process	regulation of signal transduction
E	0016020	cellular_component	membrane
E	0019904	molecular_function	protein domain specific binding
E	0022409	biological_process	positive regulation of cell-cell adhesion
E	0030971	molecular_function	receptor tyrosine kinase binding
E	0031982	cellular_component	vesicle
E	0032869	biological_process	cellular response to insulin stimulus
E	0032880	biological_process	regulation of protein localization
E	0042149	biological_process	cellular response to glucose starvation
E	0042802	molecular_function	identical protein binding
E	0045202	cellular_component	synapse
E	0045664	biological_process	regulation of neuron differentiation
E	0048167	biological_process	regulation of synaptic plasticity
E	0050870	biological_process	positive regulation of T cell activation
E	0070062	cellular_component	extracellular exosome
E	0098793	cellular_component	presynapse
E	0140031	molecular_function	phosphorylation-dependent protein binding
E	0140311	molecular_function	protein sequestering activity
E	1904262	biological_process	negative regulation of TORC1 signaling
F	0002842	biological_process	positive regulation of T cell mediated immune response to tumor cell
F	0003723	molecular_function	RNA binding
F	0005080	molecular_function	protein kinase C binding
F	0005159	molecular_function	insulin-like growth factor receptor binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005759	cellular_component	mitochondrial matrix
F	0005829	cellular_component	cytosol
F	0005925	cellular_component	focal adhesion
F	0006469	biological_process	negative regulation of protein kinase activity
F	0006605	biological_process	protein targeting
F	0007165	biological_process	signal transduction
F	0008104	biological_process	intracellular protein localization
F	0008426	molecular_function	protein kinase C inhibitor activity
F	0009966	biological_process	regulation of signal transduction
F	0016020	cellular_component	membrane
F	0019904	molecular_function	protein domain specific binding
F	0022409	biological_process	positive regulation of cell-cell adhesion
F	0030971	molecular_function	receptor tyrosine kinase binding
F	0031982	cellular_component	vesicle
F	0032869	biological_process	cellular response to insulin stimulus
F	0032880	biological_process	regulation of protein localization
F	0042149	biological_process	cellular response to glucose starvation
F	0042802	molecular_function	identical protein binding
F	0045202	cellular_component	synapse
F	0045664	biological_process	regulation of neuron differentiation
F	0048167	biological_process	regulation of synaptic plasticity
F	0050870	biological_process	positive regulation of T cell activation
F	0070062	cellular_component	extracellular exosome
F	0098793	cellular_component	presynapse
F	0140031	molecular_function	phosphorylation-dependent protein binding
F	0140311	molecular_function	protein sequestering activity
F	1904262	biological_process	negative regulation of TORC1 signaling
I	0002842	biological_process	positive regulation of T cell mediated immune response to tumor cell
I	0003723	molecular_function	RNA binding
I	0005080	molecular_function	protein kinase C binding
I	0005159	molecular_function	insulin-like growth factor receptor binding
I	0005515	molecular_function	protein binding
I	0005634	cellular_component	nucleus
I	0005737	cellular_component	cytoplasm
I	0005759	cellular_component	mitochondrial matrix
I	0005829	cellular_component	cytosol
I	0005925	cellular_component	focal adhesion
I	0006469	biological_process	negative regulation of protein kinase activity
I	0006605	biological_process	protein targeting
I	0007165	biological_process	signal transduction
I	0008104	biological_process	intracellular protein localization
I	0008426	molecular_function	protein kinase C inhibitor activity
I	0009966	biological_process	regulation of signal transduction
I	0016020	cellular_component	membrane
I	0019904	molecular_function	protein domain specific binding
I	0022409	biological_process	positive regulation of cell-cell adhesion
I	0030971	molecular_function	receptor tyrosine kinase binding
I	0031982	cellular_component	vesicle
I	0032869	biological_process	cellular response to insulin stimulus
I	0032880	biological_process	regulation of protein localization
I	0042149	biological_process	cellular response to glucose starvation
I	0042802	molecular_function	identical protein binding
I	0045202	cellular_component	synapse
I	0045664	biological_process	regulation of neuron differentiation
I	0048167	biological_process	regulation of synaptic plasticity
I	0050870	biological_process	positive regulation of T cell activation
I	0070062	cellular_component	extracellular exosome
I	0098793	cellular_component	presynapse
I	0140031	molecular_function	phosphorylation-dependent protein binding
I	0140311	molecular_function	protein sequestering activity
I	1904262	biological_process	negative regulation of TORC1 signaling
J	0002842	biological_process	positive regulation of T cell mediated immune response to tumor cell
J	0003723	molecular_function	RNA binding
J	0005080	molecular_function	protein kinase C binding
J	0005159	molecular_function	insulin-like growth factor receptor binding
J	0005515	molecular_function	protein binding
J	0005634	cellular_component	nucleus
J	0005737	cellular_component	cytoplasm
J	0005759	cellular_component	mitochondrial matrix
J	0005829	cellular_component	cytosol
J	0005925	cellular_component	focal adhesion
J	0006469	biological_process	negative regulation of protein kinase activity
J	0006605	biological_process	protein targeting
J	0007165	biological_process	signal transduction
J	0008104	biological_process	intracellular protein localization
J	0008426	molecular_function	protein kinase C inhibitor activity
J	0009966	biological_process	regulation of signal transduction
J	0016020	cellular_component	membrane
J	0019904	molecular_function	protein domain specific binding
J	0022409	biological_process	positive regulation of cell-cell adhesion
J	0030971	molecular_function	receptor tyrosine kinase binding
J	0031982	cellular_component	vesicle
J	0032869	biological_process	cellular response to insulin stimulus
J	0032880	biological_process	regulation of protein localization
J	0042149	biological_process	cellular response to glucose starvation
J	0042802	molecular_function	identical protein binding
J	0045202	cellular_component	synapse
J	0045664	biological_process	regulation of neuron differentiation
J	0048167	biological_process	regulation of synaptic plasticity
J	0050870	biological_process	positive regulation of T cell activation
J	0070062	cellular_component	extracellular exosome
J	0098793	cellular_component	presynapse
J	0140031	molecular_function	phosphorylation-dependent protein binding
J	0140311	molecular_function	protein sequestering activity
J	1904262	biological_process	negative regulation of TORC1 signaling

Functional Information from PROSITE/UniProt

site_id	PS00796
Number of Residues	11
Details	1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV

Chain	Residue	Details
A	ARG42-VAL52

---

site_id	PS00797
Number of Residues	20
Details	1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS

Chain	Residue	Details
A	TYR216-SER235

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	820
Details	Region: {"description":"Required for interaction with SPATA18/MIEAP (isoform 2) but dispensable for binding to SPATA18/MIEAP (isoform 1)","evidences":[{"source":"PubMed","id":"22532927","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Site: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"source":"PubMed","id":"17085597","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	Modified residue: {"description":"N-acetylvaline; partial","evidences":[{"source":"PubMed","id":"14534293","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P61983","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	5
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P61983","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	5
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"1377674","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25330774","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385646","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"1377674","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---