Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8UQ9

Crystal structure of RNF168 (RING)-UbcH5c fused to H2A-H2B via a 4-residue linker

Functional Information from GO Data

Chain	GOid	namespace	contents
a	0000122	biological_process	negative regulation of transcription by RNA polymerase II
a	0000166	molecular_function	nucleotide binding
a	0000209	biological_process	protein polyubiquitination
a	0000786	cellular_component	nucleosome
a	0003677	molecular_function	DNA binding
a	0004842	molecular_function	ubiquitin-protein transferase activity
a	0005515	molecular_function	protein binding
a	0005524	molecular_function	ATP binding
a	0005634	cellular_component	nucleus
a	0005654	cellular_component	nucleoplasm
a	0005829	cellular_component	cytosol
a	0005886	cellular_component	plasma membrane
a	0006281	biological_process	DNA repair
a	0006511	biological_process	ubiquitin-dependent protein catabolic process
a	0006513	biological_process	protein monoubiquitination
a	0006915	biological_process	apoptotic process
a	0006974	biological_process	DNA damage response
a	0010008	cellular_component	endosome membrane
a	0016567	biological_process	protein ubiquitination
a	0016740	molecular_function	transferase activity
a	0030514	biological_process	negative regulation of BMP signaling pathway
a	0030527	molecular_function	structural constituent of chromatin
a	0036211	biological_process	protein modification process
a	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
a	0046982	molecular_function	protein heterodimerization activity
a	0051865	biological_process	protein autoubiquitination
a	0061630	molecular_function	ubiquitin protein ligase activity
a	0061631	molecular_function	ubiquitin conjugating enzyme activity
a	0070062	cellular_component	extracellular exosome
a	0070936	biological_process	protein K48-linked ubiquitination
a	0070979	biological_process	protein K11-linked ubiquitination
a	0085020	biological_process	protein K6-linked ubiquitination
a	1903955	biological_process	obsolete positive regulation of protein targeting to mitochondrion
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000166	molecular_function	nucleotide binding
A	0000209	biological_process	protein polyubiquitination
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006281	biological_process	DNA repair
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0006513	biological_process	protein monoubiquitination
A	0006915	biological_process	apoptotic process
A	0006974	biological_process	DNA damage response
A	0010008	cellular_component	endosome membrane
A	0016567	biological_process	protein ubiquitination
A	0016740	molecular_function	transferase activity
A	0030514	biological_process	negative regulation of BMP signaling pathway
A	0030527	molecular_function	structural constituent of chromatin
A	0036211	biological_process	protein modification process
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0046982	molecular_function	protein heterodimerization activity
A	0051865	biological_process	protein autoubiquitination
A	0061630	molecular_function	ubiquitin protein ligase activity
A	0061631	molecular_function	ubiquitin conjugating enzyme activity
A	0070062	cellular_component	extracellular exosome
A	0070936	biological_process	protein K48-linked ubiquitination
A	0070979	biological_process	protein K11-linked ubiquitination
A	0085020	biological_process	protein K6-linked ubiquitination
A	1903955	biological_process	obsolete positive regulation of protein targeting to mitochondrion

Functional Information from PROSITE/UniProt

site_id	PS00046
Number of Residues	7
Details	HISTONE_H2A Histone H2A signature. AGLqFPV

Chain	Residue	Details
A	ALA3021-VAL3027

site_id	PS00183
Number of Residues	16
Details	UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL

Chain	Residue	Details
A	TYR1074-LEU1089

site_id	PS00357
Number of Residues	23
Details	HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG

Chain	Residue	Details
A	ARG2092-GLY2114

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"N6-benzoyllysine; alternate","evidences":[{"source":"PubMed","id":"30154464","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N6-isonicotinyllysine","evidences":[{"source":"PubMed","id":"34545082","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-crotonyllysine; alternate","evidences":[{"source":"PubMed","id":"21925322","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"22713238","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22980979","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"16307923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713563","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22713238","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22980979","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"UniProtKB","id":"Q64475","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by AMPK","evidences":[{"source":"UniProtKB","id":"Q64524","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"N6-isonicotinyllysine; alternate","evidences":[{"source":"PubMed","id":"34545082","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"PubMed","id":"34961760","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q00729","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"21726816","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	78
Details	Zinc finger: {"description":"RING-type","evidences":[{"source":"HAMAP-Rule","id":"MF_03066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q80XJ2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)