8ASC

Ku70/80 binds to the Ku-binding motif of PAXX

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000723	biological_process	telomere maintenance
A	0003677	molecular_function	DNA binding
A	0003678	molecular_function	DNA helicase activity
A	0003684	molecular_function	damaged DNA binding
A	0005634	cellular_component	nucleus
A	0006303	biological_process	double-strand break repair via nonhomologous end joining
A	0042162	molecular_function	telomeric DNA binding
A	0043564	cellular_component	Ku70:Ku80 complex
B	0000723	biological_process	telomere maintenance
B	0003677	molecular_function	DNA binding
B	0003678	molecular_function	DNA helicase activity
B	0003684	molecular_function	damaged DNA binding
B	0005634	cellular_component	nucleus
B	0006303	biological_process	double-strand break repair via nonhomologous end joining
B	0006310	biological_process	DNA recombination
B	0042162	molecular_function	telomeric DNA binding
B	0043564	cellular_component	Ku70:Ku80 complex
E	0000723	biological_process	telomere maintenance
E	0003677	molecular_function	DNA binding
E	0003678	molecular_function	DNA helicase activity
E	0003684	molecular_function	damaged DNA binding
E	0005634	cellular_component	nucleus
E	0006303	biological_process	double-strand break repair via nonhomologous end joining
E	0042162	molecular_function	telomeric DNA binding
E	0043564	cellular_component	Ku70:Ku80 complex
F	0000723	biological_process	telomere maintenance
F	0003677	molecular_function	DNA binding
F	0003678	molecular_function	DNA helicase activity
F	0003684	molecular_function	damaged DNA binding
F	0005634	cellular_component	nucleus
F	0006303	biological_process	double-strand break repair via nonhomologous end joining
F	0006310	biological_process	DNA recombination
F	0042162	molecular_function	telomeric DNA binding
F	0043564	cellular_component	Ku70:Ku80 complex
J	0006303	biological_process	double-strand break repair via nonhomologous end joining
K	0000723	biological_process	telomere maintenance
K	0003677	molecular_function	DNA binding
K	0003678	molecular_function	DNA helicase activity
K	0003684	molecular_function	damaged DNA binding
K	0005634	cellular_component	nucleus
K	0006303	biological_process	double-strand break repair via nonhomologous end joining
K	0042162	molecular_function	telomeric DNA binding
K	0043564	cellular_component	Ku70:Ku80 complex
L	0000723	biological_process	telomere maintenance
L	0003677	molecular_function	DNA binding
L	0003678	molecular_function	DNA helicase activity
L	0003684	molecular_function	damaged DNA binding
L	0005634	cellular_component	nucleus
L	0006303	biological_process	double-strand break repair via nonhomologous end joining
L	0006310	biological_process	DNA recombination
L	0042162	molecular_function	telomeric DNA binding
L	0043564	cellular_component	Ku70:Ku80 complex
O	0000723	biological_process	telomere maintenance
O	0003677	molecular_function	DNA binding
O	0003678	molecular_function	DNA helicase activity
O	0003684	molecular_function	damaged DNA binding
O	0005634	cellular_component	nucleus
O	0006303	biological_process	double-strand break repair via nonhomologous end joining
O	0042162	molecular_function	telomeric DNA binding
O	0043564	cellular_component	Ku70:Ku80 complex
P	0000723	biological_process	telomere maintenance
P	0003677	molecular_function	DNA binding
P	0003678	molecular_function	DNA helicase activity
P	0003684	molecular_function	damaged DNA binding
P	0005634	cellular_component	nucleus
P	0006303	biological_process	double-strand break repair via nonhomologous end joining
P	0006310	biological_process	DNA recombination
P	0042162	molecular_function	telomeric DNA binding
P	0043564	cellular_component	Ku70:Ku80 complex
T	0006303	biological_process	double-strand break repair via nonhomologous end joining

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
B	LYS144
P	LYS144
P	LYS265
P	LYS332
B	LYS265
B	LYS332
F	LYS144
F	LYS265
F	LYS332
L	LYS144
L	LYS265
L	LYS332

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
B	SER255
P	SER255
P	SER258
P	SER318
B	SER258
B	SER318
F	SER255
F	SER258
F	SER318
L	SER255
L	SER258
L	SER318

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
B	THR535
F	THR535
L	THR535
P	THR535

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
B	LYS195
K	LYS331
L	LYS532
L	LYS534
P	LYS195
O	LYS331
P	LYS532
P	LYS534
A	LYS331
B	LYS532
B	LYS534
F	LYS195
E	LYS331
F	LYS532
F	LYS534
L	LYS195

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PRKDC => ECO:0000269|PubMed:9362500

Chain	Residue	Details
A	SER51
E	SER51
K	SER51
O	SER51

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR455
E	THR455
K	THR455
O	THR455

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER477
E	SER477
K	SER477
O	SER477

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER520
E	SER520
K	SER520
O	SER520

---

site_id	SWS_FT_FI9
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS287
O	LYS287
O	LYS317
A	LYS317
E	LYS287
E	LYS317
K	LYS287
K	LYS317

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