3UZD

Crystal structure of 14-3-3 GAMMA

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0005737	cellular_component	cytoplasm
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	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	0030971	molecular_function	receptor tyrosine kinase binding
A	0031982	cellular_component	vesicle
A	0032869	biological_process	cellular response to insulin stimulus
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	0050815	molecular_function	phosphoserine residue binding
A	0070062	cellular_component	extracellular exosome
A	0098793	cellular_component	presynapse
A	0140311	molecular_function	protein sequestering activity
A	1904262	biological_process	negative regulation of TORC1 signaling

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 A 301

Chain	Residue
A	SER113
A	GLU114
A	THR115
A	ALA189
A	PRO190
A	GLU191
A	GLN192

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 A 302

Chain	Residue
A	TYR216
A	LYS217
A	ASP218
A	HOH429
A	ASP214
A	SER215

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 303

Chain	Residue
A	HOH459
A	HOH480

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NO3 B 101

Chain	Residue
A	GLU185
B	PRO7

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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	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	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:22649097, ECO:0007744|PubMed:19690332

Chain	Residue	Details
B	SEP8
A	ARG132

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial => ECO:0000269|Ref.7

Chain	Residue	Details
A	MET1

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylvaline; partial => ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330

Chain	Residue	Details
A	VAL2

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER71

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P61983

Chain	Residue	Details
A	TYR133

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|Ref.7

Chain	Residue	Details
A	THR145

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P61983

Chain	Residue	Details
A	SER215

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR234

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER235

---