9EBS

Cryo-EM structure of USP1-UAF1-Ubiquitin in complex with TNG348

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
D	0000724	biological_process	double-strand break repair via homologous recombination
D	0003677	molecular_function	DNA binding
D	0003690	molecular_function	double-stranded DNA binding
D	0003697	molecular_function	single-stranded DNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005764	cellular_component	lysosome
D	0005770	cellular_component	late endosome
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006281	biological_process	DNA repair
D	0006974	biological_process	DNA damage response
D	0035800	molecular_function	deubiquitinase activator activity
D	0043130	molecular_function	ubiquitin binding
D	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
D	0060255	biological_process	regulation of macromolecule metabolic process
D	0080090	biological_process	regulation of primary metabolic process
D	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
D	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
E	0004197	molecular_function	cysteine-type endopeptidase activity
E	0004843	molecular_function	cysteine-type deubiquitinase activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005829	cellular_component	cytosol
E	0006281	biological_process	DNA repair
E	0006282	biological_process	regulation of DNA repair
E	0006508	biological_process	proteolysis
E	0006974	biological_process	DNA damage response
E	0008233	molecular_function	peptidase activity
E	0008234	molecular_function	cysteine-type peptidase activity
E	0009411	biological_process	response to UV
E	0016579	biological_process	protein deubiquitination
E	0016787	molecular_function	hydrolase activity
E	0031647	biological_process	regulation of protein stability
E	0035520	biological_process	monoubiquitinated protein deubiquitination
E	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
E	1904333	biological_process	positive regulation of error-prone translesion synthesis

Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LISAssDtTVKVWNA

Chain	Residue	Details
D	LEU90-ALA104
D	VAL132-VAL146

---

site_id	PS00972
Number of Residues	16
Details	USP_1 Ubiquitin specific protease (USP) domain signature 1. GLnnlGNtCYLNSiLQ

Chain	Residue	Details
E	GLY82-GLN97

---

site_id	PS00973
Number of Residues	19
Details	USP_2 Ubiquitin specific protease (USP) domain signature 2. YgLfAVvmHsGitiss.GHY

Chain	Residue	Details
E	TYR576-TYR594

---

site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD

Chain	Residue	Details
C	LYS27-ASP52

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	39
Details	Repeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	39
Details	Repeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	39
Details	Repeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	39
Details	Repeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	39
Details	Repeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	39
Details	Repeat: {"description":"WD 8","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BH57","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15694335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16531995","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26388029","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BJQ2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---