6YIA

14-3-3 sigma in complex with SMAD2 pS465 peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0001836	biological_process	release of cytochrome c from mitochondria
A	0003334	biological_process	keratinocyte development
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006469	biological_process	negative regulation of protein kinase activity
A	0006611	biological_process	protein export from nucleus
A	0007165	biological_process	signal transduction
A	0008104	biological_process	protein localization
A	0008426	molecular_function	protein kinase C inhibitor activity
A	0008630	biological_process	intrinsic apoptotic signaling pathway in response to DNA damage
A	0010482	biological_process	regulation of epidermal cell division
A	0010839	biological_process	negative regulation of keratinocyte proliferation
A	0019901	molecular_function	protein kinase binding
A	0022407	biological_process	regulation of cell-cell adhesion
A	0030216	biological_process	keratinocyte differentiation
A	0030307	biological_process	positive regulation of cell growth
A	0031424	biological_process	keratinization
A	0032880	biological_process	regulation of protein localization
A	0042742	biological_process	defense response to bacterium
A	0042802	molecular_function	identical protein binding
A	0043588	biological_process	skin development
A	0043616	biological_process	keratinocyte proliferation
A	0045296	molecular_function	cadherin binding
A	0045606	biological_process	positive regulation of epidermal cell differentiation
A	0045785	biological_process	positive regulation of cell adhesion
A	0045824	biological_process	negative regulation of innate immune response
A	0046827	biological_process	positive regulation of protein export from nucleus
A	0050815	molecular_function	phosphoserine residue binding
A	0051219	molecular_function	phosphoprotein binding
A	0051715	biological_process	cytolysis in another organism
A	0051726	biological_process	regulation of cell cycle
A	0061436	biological_process	establishment of skin barrier
A	0070062	cellular_component	extracellular exosome
A	0072089	biological_process	stem cell proliferation
A	0140311	molecular_function	protein sequestering activity
A	0141156	biological_process	cAMP/PKA signal transduction
A	0160075	biological_process	non-canonical inflammasome complex assembly
A	1903077	biological_process	negative regulation of protein localization to plasma membrane
A	1903829	biological_process	positive regulation of protein localization
A	2000647	biological_process	negative regulation of stem cell proliferation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 301

Chain	Residue
A	GLU89
A	VAL134
A	THR136
A	HOH574
A	HOH717

---

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 302

Chain	Residue
A	HOH703
A	HOH729
A	GLU75
A	GLU161
A	HOH653
A	HOH660

---

site_id	AC3
Number of Residues	10
Details	binding site for residue MG A 303

Chain	Residue
A	GLU2
A	GLU2
A	HOH594
A	HOH594
A	HOH641
A	HOH641
A	HOH649
A	HOH649
A	HOH727
A	HOH727

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MG A 304

Chain	Residue
A	ARG18
A	GLU20
A	ASP21
A	HOH599
A	HOH613

---

site_id	AC5
Number of Residues	5
Details	binding site for residue MG A 305

Chain	Residue
A	LYS124
A	ALA150
A	GLU153
A	HOH490
A	HOH536

---

site_id	AC6
Number of Residues	5
Details	binding site for residue GOL A 306

Chain	Residue
A	TYR213
A	THR217
A	MET220
A	ARG224
A	HOH402

---

site_id	AC7
Number of Residues	3
Details	binding site for residue CL A 307

Chain	Residue
A	LYS9
A	HOH743
A	HOH767

---

site_id	AC8
Number of Residues	6
Details	binding site for residue CA A 308

Chain	Residue
A	GLU35
A	GLU110
A	GLU188
A	HOH576
A	HOH655
A	HOH724

---

site_id	AC9
Number of Residues	3
Details	binding site for residue NA A 309

Chain	Residue
A	SER146
A	HOH497
A	HOH536

---

site_id	AD1
Number of Residues	14
Details	binding site for Ligand residues SEP P 127 through MET P 128 bound to SER P 126

Chain	Residue
A	LYS49
A	ARG56
A	ARG129
A	TYR130
A	LEU174
A	ASN175
P	SER126
P	SER129
P	HOH203
P	HOH204
P	HOH206
P	HOH209
P	HOH211
P	HOH213

---

site_id	AD2
Number of Residues	14
Details	binding site for Ligand SEP P 127 bound to SER P 126

Chain	Residue
A	LYS49
A	ARG56
A	ARG129
A	TYR130
A	ASN175
P	SER126
P	MET128
P	SER129
P	HOH203
P	HOH204
P	HOH206
P	HOH209
P	HOH211
P	HOH213

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
P	SER122
A	ARG129

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000255|PROSITE-ProRule:PRU00439, ECO:0000269|PubMed:8980228

Chain	Residue	Details
P	SER126

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by TGFBR1 => ECO:0000255|PROSITE-ProRule:PRU00439, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:8980228, ECO:0000269|PubMed:9136927, ECO:0000269|PubMed:9346908

Chain	Residue	Details
P	SEP127
P	SER129

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