Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8E0Q

Structure of the human UBR5 HECT-type E3 ubiquitin ligase in a C2 symmetric dimeric form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000209	biological_process	protein polyubiquitination
A	0000785	cellular_component	chromatin
A	0003723	molecular_function	RNA binding
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006281	biological_process	DNA repair
A	0006974	biological_process	DNA damage response
A	0006979	biological_process	response to oxidative stress
A	0008270	molecular_function	zinc ion binding
A	0010498	biological_process	proteasomal protein catabolic process
A	0010628	biological_process	positive regulation of gene expression
A	0016020	cellular_component	membrane
A	0016567	biological_process	protein ubiquitination
A	0016740	molecular_function	transferase activity
A	0030520	biological_process	estrogen receptor signaling pathway
A	0032991	cellular_component	protein-containing complex
A	0033696	biological_process	heterochromatin boundary formation
A	0034450	molecular_function	ubiquitin-ubiquitin ligase activity
A	0035519	biological_process	protein K29-linked ubiquitination
A	0042307	biological_process	positive regulation of protein import into nucleus
A	0043130	molecular_function	ubiquitin binding
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0045879	biological_process	negative regulation of smoothened signaling pathway
A	0046872	molecular_function	metal ion binding
A	0048384	biological_process	retinoic acid receptor signaling pathway
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050847	biological_process	progesterone receptor signaling pathway
A	0061630	molecular_function	ubiquitin protein ligase activity
A	0070561	biological_process	vitamin D receptor signaling pathway
A	0070936	biological_process	protein K48-linked ubiquitination
A	0070979	biological_process	protein K11-linked ubiquitination
A	0071629	biological_process	cytoplasm protein quality control by the ubiquitin-proteasome system
A	0071630	biological_process	nuclear protein quality control by the ubiquitin-proteasome system
A	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
A	0140455	biological_process	cytoplasm protein quality control
A	0140861	biological_process	DNA repair-dependent chromatin remodeling
A	0141198	biological_process	protein branched polyubiquitination
B	0000209	biological_process	protein polyubiquitination
B	0000785	cellular_component	chromatin
B	0003723	molecular_function	RNA binding
B	0004842	molecular_function	ubiquitin-protein transferase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006281	biological_process	DNA repair
B	0006974	biological_process	DNA damage response
B	0006979	biological_process	response to oxidative stress
B	0008270	molecular_function	zinc ion binding
B	0010498	biological_process	proteasomal protein catabolic process
B	0010628	biological_process	positive regulation of gene expression
B	0016020	cellular_component	membrane
B	0016567	biological_process	protein ubiquitination
B	0016740	molecular_function	transferase activity
B	0030520	biological_process	estrogen receptor signaling pathway
B	0032991	cellular_component	protein-containing complex
B	0033696	biological_process	heterochromatin boundary formation
B	0034450	molecular_function	ubiquitin-ubiquitin ligase activity
B	0035519	biological_process	protein K29-linked ubiquitination
B	0042307	biological_process	positive regulation of protein import into nucleus
B	0043130	molecular_function	ubiquitin binding
B	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
B	0045879	biological_process	negative regulation of smoothened signaling pathway
B	0046872	molecular_function	metal ion binding
B	0048384	biological_process	retinoic acid receptor signaling pathway
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050847	biological_process	progesterone receptor signaling pathway
B	0061630	molecular_function	ubiquitin protein ligase activity
B	0070561	biological_process	vitamin D receptor signaling pathway
B	0070936	biological_process	protein K48-linked ubiquitination
B	0070979	biological_process	protein K11-linked ubiquitination
B	0071629	biological_process	cytoplasm protein quality control by the ubiquitin-proteasome system
B	0071630	biological_process	nuclear protein quality control by the ubiquitin-proteasome system
B	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
B	0140455	biological_process	cytoplasm protein quality control
B	0140861	biological_process	DNA repair-dependent chromatin remodeling
B	0141198	biological_process	protein branched polyubiquitination

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	136
Details	Zinc finger: {"description":"UBR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00508","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00104","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11287654","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23027739","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28689657","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"37040767","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"37478862","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"37620400","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37040767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37409633","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37478846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37620400","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BJA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8C06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8D4X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8E0Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8EWI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8P82","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	22
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21924388","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21924388","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21924388","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)