Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8UQC

Crystal structure of RNF168 (RING)-UbcH5c fused to H2A-H2B via a 20-residue linker (crystallization condition 2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000151	cellular_component	ubiquitin ligase complex
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	0005768	cellular_component	endosome
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	0010008	cellular_component	endosome membrane
A	0016567	biological_process	protein ubiquitination
A	0016740	molecular_function	transferase activity
A	0019787	molecular_function	ubiquitin-like protein transferase activity
A	0030514	biological_process	negative regulation of BMP signaling pathway
A	0030527	molecular_function	structural constituent of chromatin
A	0031625	molecular_function	ubiquitin protein ligase binding
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	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	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	39
Details	ZN_FING: RING-type => ECO:0000255\|HAMAP-Rule:MF_03066

Chain	Residue	Details
A	CYS16-ARG55

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q80XJ2

Chain	Residue	Details
A	SER70

site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Glycyl thioester intermediate => ECO:0000255\|PROSITE-ProRule:PRU00388, ECO:0000255\|PROSITE-ProRule:PRU10133

Chain	Residue	Details
A	LYS1085

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435

Chain	Residue	Details
A	LYS2034
A	LYS2116
A	LYS2120
A	LYS3095

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250\|UniProtKB:Q64475

Chain	Residue	Details
A	GLU2035

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by AMPK => ECO:0000250\|UniProtKB:Q64524

Chain	Residue	Details
A	SER2036

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-lactoyllysine; alternate => ECO:0000269\|PubMed:31645732

Chain	Residue	Details
A	LYS2043
A	LYS2085

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:16627869

Chain	Residue	Details
A	LYS2046
A	LYS2108

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269\|PubMed:24681537

Chain	Residue	Details
A	LYS2057

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Dimethylated arginine => ECO:0000250\|UniProtKB:Q96A08

Chain	Residue	Details
A	ARG2079

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:Q96A08

Chain	Residue	Details
A	ARG2086
A	ARG2092

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q00729

Chain	Residue	Details
A	THR2115

site_id	SWS_FT_FI13
Number of Residues	1
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250\|UniProtKB:P62807

Chain	Residue	Details
A	SER2112

site_id	SWS_FT_FI14
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:21726816

Chain	Residue	Details
A	LYS2034

site_id	SWS_FT_FI15
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:22713238, ECO:0000269\|PubMed:22980979

Chain	Residue	Details
A	LYS3015

site_id	SWS_FT_FI16
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:16307923, ECO:0000269\|PubMed:16627869, ECO:0000269\|PubMed:16713563

Chain	Residue	Details
A	LYS2120

site_id	SWS_FT_FI17
Number of Residues	1
Details	MOD_RES: N6-(beta-hydroxybutyryl)lysine; alternate => ECO:0000269\|PubMed:27105115

Chain	Residue	Details
A	LYS3013

site_id	SWS_FT_FI18
Number of Residues	1
Details	MOD_RES: N6-crotonyllysine; alternate => ECO:0000269\|PubMed:21925322

Chain	Residue	Details
A	LYS3036

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:24681537

Chain	Residue	Details
A	LYS3074
A	LYS3075

site_id	SWS_FT_FI20
Number of Residues	1
Details	MOD_RES: N5-methylglutamine => ECO:0000269\|PubMed:24352239

Chain	Residue	Details
A	GLN3104

site_id	SWS_FT_FI21
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:22713238, ECO:0000269\|PubMed:22980979

Chain	Residue	Details
A	LYS3013

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