5N10

Cucurbit[8]uril and 14-3-3 based binary bivalent supramolecular-protein assembly platform

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004860	molecular_function	protein kinase inhibitor activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005773	cellular_component	vacuole
A	0005774	cellular_component	vacuolar membrane
A	0005829	cellular_component	cytosol
A	0005925	cellular_component	focal adhesion
A	0006605	biological_process	protein targeting
A	0007165	biological_process	signal transduction
A	0008104	biological_process	protein localization
A	0016020	cellular_component	membrane
A	0019899	molecular_function	enzyme binding
A	0019904	molecular_function	protein domain specific binding
A	0035308	biological_process	negative regulation of protein dephosphorylation
A	0042470	cellular_component	melanosome
A	0042802	molecular_function	identical protein binding
A	0042826	molecular_function	histone deacetylase binding
A	0043085	biological_process	positive regulation of catalytic activity
A	0045296	molecular_function	cadherin binding
A	0045744	biological_process	negative regulation of G protein-coupled receptor signaling pathway
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050815	molecular_function	phosphoserine residue binding
A	0051219	molecular_function	phosphoprotein binding
A	0051220	biological_process	cytoplasmic sequestering of protein
A	0070062	cellular_component	extracellular exosome
B	0004860	molecular_function	protein kinase inhibitor activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005773	cellular_component	vacuole
B	0005774	cellular_component	vacuolar membrane
B	0005829	cellular_component	cytosol
B	0005925	cellular_component	focal adhesion
B	0006605	biological_process	protein targeting
B	0007165	biological_process	signal transduction
B	0008104	biological_process	protein localization
B	0016020	cellular_component	membrane
B	0019899	molecular_function	enzyme binding
B	0019904	molecular_function	protein domain specific binding
B	0035308	biological_process	negative regulation of protein dephosphorylation
B	0042470	cellular_component	melanosome
B	0042802	molecular_function	identical protein binding
B	0042826	molecular_function	histone deacetylase binding
B	0043085	biological_process	positive regulation of catalytic activity
B	0045296	molecular_function	cadherin binding
B	0045744	biological_process	negative regulation of G protein-coupled receptor signaling pathway
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050815	molecular_function	phosphoserine residue binding
B	0051219	molecular_function	phosphoprotein binding
B	0051220	biological_process	cytoplasmic sequestering of protein
B	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue GOL A 301

Chain	Residue
A	LYS195
A	PHE198
A	ASP199
A	ARG224
A	HOH467
A	HOH469
A	HOH548

---

site_id	AC2
Number of Residues	23
Details	binding site for residue C8L C 601

Chain	Residue
A	GLU233
B	GLN69
B	THR71
C	PHE581
C	GLY582
C	GLU587
C	GLU589
C	GLY590
C	HOH702
C	HOH704
C	HOH705
C	HOH713
C	HOH715
C	HOH723
C	HOH725
C	HOH727
C	HOH730
D	PHE581
D	GLY582
D	GLY583
D	HOH601
A	LEU229
A	SER232

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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	ARG43-VAL53
B	ARG43-VAL53

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

Chain	Residue	Details
A	TYR213-SER232
B	TYR213-SER232

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Interaction with phosphoserine on interacting protein => ECO:0000250

Chain	Residue	Details
B	ARG58
B	ARG129

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate => ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378

Chain	Residue	Details
B	MET1

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
B	THR2

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27348

Chain	Residue	Details
B	LYS5

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P27348

Chain	Residue	Details
B	LYS51

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CQV8

Chain	Residue	Details
B	SER60

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
B	LYS70
B	LYS117

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q9CQV8

Chain	Residue	Details
B	TYR84
B	TYR106

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68251

Chain	Residue	Details
B	SER186

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site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
B	SER232

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site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P27348

Chain	Residue	Details
B	LYS51

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