8SRP
FoxP3 forms Ladder-like multimer to bridge TTTG repeats
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0043565 | molecular_function | sequence-specific DNA binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0043565 | molecular_function | sequence-specific DNA binding |
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 |
E | 0003700 | molecular_function | DNA-binding transcription factor activity |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0043565 | molecular_function | sequence-specific DNA binding |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 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 |
I | 0003700 | molecular_function | DNA-binding transcription factor activity |
I | 0006355 | biological_process | regulation of DNA-templated transcription |
I | 0043565 | molecular_function | sequence-specific DNA binding |
J | 0003700 | molecular_function | DNA-binding transcription factor activity |
J | 0006355 | biological_process | regulation of DNA-templated transcription |
J | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 250 |
Details | ZN_FING: C2H2-type |
Chain | Residue | Details |
A | GLY196-HIS221 | |
I | GLY196-HIS221 | |
J | GLY196-HIS221 | |
H | GLY196-HIS221 | |
G | GLY196-HIS221 | |
F | GLY196-HIS221 | |
E | GLY196-HIS221 | |
D | GLY196-HIS221 | |
C | GLY196-HIS221 | |
B | GLY196-HIS221 |
site_id | SWS_FT_FI2 |
Number of Residues | 860 |
Details | DNA_BIND: Fork-head => ECO:0000255|PROSITE-ProRule:PRU00089 |
Chain | Residue | Details |
A | ARG337-LYS423 | |
I | ARG337-LYS423 | |
J | ARG337-LYS423 | |
H | ARG337-LYS423 | |
G | ARG337-LYS423 | |
F | ARG337-LYS423 | |
E | ARG337-LYS423 | |
D | ARG337-LYS423 | |
C | ARG337-LYS423 | |
B | ARG337-LYS423 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | SITE: Cleavage; by PCSK1 or PCSK2 => ECO:0000269|PubMed:19117830 |
Chain | Residue | Details |
A | ARG417 | |
I | ARG417 | |
J | ARG417 | |
H | ARG417 | |
G | ARG417 | |
F | ARG417 | |
E | ARG417 | |
D | ARG417 | |
C | ARG417 | |
B | ARG417 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:22312127 |
Chain | Residue | Details |
A | LYS262 | |
A | LYS267 | |
I | LYS262 | |
I | LYS267 | |
J | LYS262 | |
J | LYS267 | |
H | LYS262 | |
H | LYS267 | |
G | LYS262 | |
G | LYS267 | |
F | LYS262 | |
F | LYS267 | |
E | LYS262 | |
E | LYS267 | |
D | LYS262 | |
D | LYS267 | |
C | LYS262 | |
C | LYS267 | |
B | LYS262 | |
B | LYS267 |
site_id | SWS_FT_FI5 |
Number of Residues | 10 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9BZS1 |
Chain | Residue | Details |
A | SER418 | |
I | SER418 | |
J | SER418 | |
H | SER418 | |
G | SER418 | |
F | SER418 | |
E | SER418 | |
D | SER418 | |
C | SER418 | |
B | SER418 |
site_id | SWS_FT_FI6 |
Number of Residues | 40 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23973222 |
Chain | Residue | Details |
A | LYS249 | |
A | LYS251 | |
A | LYS393 | |
I | LYS249 | |
I | LYS251 | |
I | LYS393 | |
J | LYS249 | |
J | LYS251 | |
J | LYS393 | |
H | LYS249 | |
H | LYS251 | |
H | LYS393 | |
G | LYS249 | |
G | LYS251 | |
G | LYS393 | |
F | LYS249 | |
F | LYS251 | |
F | LYS393 | |
E | LYS249 | |
E | LYS251 | |
E | LYS393 | |
D | LYS249 | |
D | LYS251 | |
D | LYS393 | |
C | LYS249 | |
C | LYS251 | |
C | LYS393 | |
B | LYS249 | |
B | LYS251 | |
B | LYS393 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:23973222 |
Chain | Residue | Details |
A | LYS262 | |
A | LYS267 | |
I | LYS262 | |
I | LYS267 | |
J | LYS262 | |
J | LYS267 | |
H | LYS262 | |
H | LYS267 | |
G | LYS262 | |
G | LYS267 | |
F | LYS262 | |
F | LYS267 | |
E | LYS262 | |
E | LYS267 | |
D | LYS262 | |
D | LYS267 | |
C | LYS262 | |
C | LYS267 | |
B | LYS262 | |
B | LYS267 |