6LBI

Crystal Structure of FOXO1-DBD homodimer bound to a palindromic DNA sequence

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0003700	molecular_function	DNA-binding transcription factor activity
C	0006355	biological_process	regulation of DNA-templated transcription
C	0043565	molecular_function	sequence-specific DNA binding
D	0003700	molecular_function	DNA-binding transcription factor activity
D	0006355	biological_process	regulation of DNA-templated transcription
D	0043565	molecular_function	sequence-specific DNA binding
G	0003700	molecular_function	DNA-binding transcription factor activity
G	0006355	biological_process	regulation of DNA-templated transcription
G	0043565	molecular_function	sequence-specific DNA binding
H	0003700	molecular_function	DNA-binding transcription factor activity
H	0006355	biological_process	regulation of DNA-templated transcription
H	0043565	molecular_function	sequence-specific DNA binding
K	0003700	molecular_function	DNA-binding transcription factor activity
K	0006355	biological_process	regulation of DNA-templated transcription
K	0043565	molecular_function	sequence-specific DNA binding
L	0003700	molecular_function	DNA-binding transcription factor activity
L	0006355	biological_process	regulation of DNA-templated transcription
L	0043565	molecular_function	sequence-specific DNA binding

Functional Information from PROSITE/UniProt

site_id	PS00658
Number of Residues	7
Details	FORK_HEAD_2 Fork head domain signature 2. WKNSIRH

Chain	Residue	Details
C	TRP209-HIS215

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	456
Details	DNA_BIND: Fork-head => ECO:0000255|PROSITE-ProRule:PRU00089

Chain	Residue	Details
C	ALA159-SER235
D	ALA159-SER235
G	ALA159-SER235
H	ALA159-SER235
K	ALA159-SER235
L	ALA159-SER235

---

site_id	SWS_FT_FI2
Number of Residues	18
Details	SITE: DNA-binding => ECO:0000269|PubMed:18786403

Chain	Residue	Details
C	ASN158
H	ASN158
H	TYR165
H	ARG225
K	ASN158
K	TYR165
K	ARG225
L	ASN158
L	TYR165
L	ARG225
C	TYR165
C	ARG225
D	ASN158
D	TYR165
D	ARG225
G	ASN158
G	TYR165
G	ARG225

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:18786403, ECO:0000269|PubMed:19221179, ECO:0000269|PubMed:21245099

Chain	Residue	Details
C	SER212
D	SER212
G	SER212
H	SER212
K	SER212
L	SER212

---

site_id	SWS_FT_FI4
Number of Residues	18
Details	MOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:18786403

Chain	Residue	Details
C	SER218
H	SER218
H	SER234
H	SER235
K	SER218
K	SER234
K	SER235
L	SER218
L	SER234
L	SER235
C	SER234
C	SER235
D	SER218
D	SER234
D	SER235
G	SER218
G	SER234
G	SER235

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9R1E0

Chain	Residue	Details
C	LYS245
K	LYS248
L	LYS245
L	LYS248
C	LYS248
D	LYS245
D	LYS248
G	LYS245
G	LYS248
H	LYS245
H	LYS248
K	LYS245

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:18356527

Chain	Residue	Details
C	SER249
D	SER249
G	SER249
H	SER249
K	SER249
L	SER249

---

site_id	SWS_FT_FI7
Number of Residues	12
Details	MOD_RES: Omega-N-methylarginine; by PRMT1 => ECO:0000250|UniProtKB:Q9R1E0

Chain	Residue	Details
C	ARG251
K	ARG253
L	ARG251
L	ARG253
C	ARG253
D	ARG251
D	ARG253
G	ARG251
G	ARG253
H	ARG251
H	ARG253
K	ARG251

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	MOD_RES: Phosphoserine; by PKB/AKT1 and SGK1 => ECO:0000269|PubMed:10358075, ECO:0000269|PubMed:10358076, ECO:0000269|PubMed:11237865, ECO:0000269|PubMed:11980723, ECO:0000269|PubMed:31063815

Chain	Residue	Details
C	SER256
D	SER256
G	SER256
H	SER256
K	SER256
L	SER256

---

site_id	SWS_FT_FI9
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:20543840

Chain	Residue	Details
C	LYS262
K	LYS265
L	LYS262
L	LYS265
C	LYS265
D	LYS262
D	LYS265
G	LYS262
G	LYS265
H	LYS262
H	LYS265
K	LYS262

---