6BD1

Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at S366

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005925	cellular_component	focal adhesion
A	0007165	biological_process	signal transduction
A	0008104	biological_process	intracellular protein localization
A	0016020	cellular_component	membrane
A	0019904	molecular_function	protein domain specific binding
A	0021762	biological_process	substantia nigra development
A	0032991	cellular_component	protein-containing complex
A	0034766	biological_process	negative regulation of monoatomic ion transmembrane transport
A	0042802	molecular_function	identical protein binding
A	0044325	molecular_function	transmembrane transporter binding
A	0045202	cellular_component	synapse
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0070062	cellular_component	extracellular exosome
A	0071889	molecular_function	14-3-3 protein binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005925	cellular_component	focal adhesion
B	0007165	biological_process	signal transduction
B	0008104	biological_process	intracellular protein localization
B	0016020	cellular_component	membrane
B	0019904	molecular_function	protein domain specific binding
B	0021762	biological_process	substantia nigra development
B	0032991	cellular_component	protein-containing complex
B	0034766	biological_process	negative regulation of monoatomic ion transmembrane transport
B	0042802	molecular_function	identical protein binding
B	0044325	molecular_function	transmembrane transporter binding
B	0045202	cellular_component	synapse
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0070062	cellular_component	extracellular exosome
B	0071889	molecular_function	14-3-3 protein binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005925	cellular_component	focal adhesion
E	0007165	biological_process	signal transduction
E	0008104	biological_process	intracellular protein localization
E	0016020	cellular_component	membrane
E	0019904	molecular_function	protein domain specific binding
E	0021762	biological_process	substantia nigra development
E	0032991	cellular_component	protein-containing complex
E	0034766	biological_process	negative regulation of monoatomic ion transmembrane transport
E	0042802	molecular_function	identical protein binding
E	0044325	molecular_function	transmembrane transporter binding
E	0045202	cellular_component	synapse
E	0045892	biological_process	negative regulation of DNA-templated transcription
E	0070062	cellular_component	extracellular exosome
E	0071889	molecular_function	14-3-3 protein binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005925	cellular_component	focal adhesion
F	0007165	biological_process	signal transduction
F	0008104	biological_process	intracellular protein localization
F	0016020	cellular_component	membrane
F	0019904	molecular_function	protein domain specific binding
F	0021762	biological_process	substantia nigra development
F	0032991	cellular_component	protein-containing complex
F	0034766	biological_process	negative regulation of monoatomic ion transmembrane transport
F	0042802	molecular_function	identical protein binding
F	0044325	molecular_function	transmembrane transporter binding
F	0045202	cellular_component	synapse
F	0045892	biological_process	negative regulation of DNA-templated transcription
F	0070062	cellular_component	extracellular exosome
F	0071889	molecular_function	14-3-3 protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue MG A 300

Chain	Residue
A	GLU84
A	GLU87
A	HOH479

---

site_id	AC2
Number of Residues	8
Details	binding site for residue 1PE A 301

Chain	Residue
B	ASP81
B	LYS85
A	GLU2
A	LEU6
A	LYS9
A	ASP21
A	THR24
A	HOH404

---

site_id	AC3
Number of Residues	6
Details	binding site for residue MG B 300

Chain	Residue
A	HOH416
A	HOH477
B	ASP81
B	GLU84
B	HOH411
B	HOH434

---

site_id	AC4
Number of Residues	3
Details	binding site for residue PEG B 301

Chain	Residue
B	ASP20
B	THR24
B	HOH493

---

site_id	AC5
Number of Residues	7
Details	binding site for residue PEG B 302

Chain	Residue
B	THR95
B	LEU98
B	ASP102
B	PHE126
F	GLN32
F	GLY33
F	ALA34

---

site_id	AC6
Number of Residues	7
Details	binding site for residue 1PE E 301

Chain	Residue
E	MET1
E	LYS9
E	ASP21
E	THR24
E	HOH466
F	ASP81
F	LYS85

---

site_id	AC7
Number of Residues	4
Details	binding site for residue PEG E 302

Chain	Residue
E	THR4
E	ILE7
E	GLN8
E	LYS11

---

site_id	AC8
Number of Residues	5
Details	binding site for residue MG F 300

Chain	Residue
E	HOH465
F	ASP81
F	GLU84
F	HOH406
F	HOH473

---

site_id	AC9
Number of Residues	3
Details	binding site for residue PEG F 301

Chain	Residue
F	ASP20
F	ARG55
F	ILE93

---

site_id	AD1
Number of Residues	4
Details	binding site for residue PEG F 302

Chain	Residue
E	ARG18
F	GLY54
F	ARG55
F	ALA58

---

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	ARG41-VAL51

---

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

Chain	Residue	Details
A	TYR211-SER230

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Site: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68254","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---