Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8GRQ

Cryo-EM structure of BRCA1/BARD1 bound to H2AK127-UbcH5c-Ub nucleosome

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0030527	molecular_function	structural constituent of chromatin
A	0046982	molecular_function	protein heterodimerization activity
B	0003677	molecular_function	DNA binding
B	0030527	molecular_function	structural constituent of chromatin
B	0046982	molecular_function	protein heterodimerization activity
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0030527	molecular_function	structural constituent of chromatin
C	0046982	molecular_function	protein heterodimerization activity
D	0000786	cellular_component	nucleosome
D	0003677	molecular_function	DNA binding
D	0030527	molecular_function	structural constituent of chromatin
D	0046982	molecular_function	protein heterodimerization activity
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0030527	molecular_function	structural constituent of chromatin
E	0046982	molecular_function	protein heterodimerization activity
F	0003677	molecular_function	DNA binding
F	0030527	molecular_function	structural constituent of chromatin
F	0046982	molecular_function	protein heterodimerization activity
G	0000786	cellular_component	nucleosome
G	0003677	molecular_function	DNA binding
G	0030527	molecular_function	structural constituent of chromatin
G	0046982	molecular_function	protein heterodimerization activity
H	0000786	cellular_component	nucleosome
H	0003677	molecular_function	DNA binding
H	0030527	molecular_function	structural constituent of chromatin
H	0046982	molecular_function	protein heterodimerization activity
K	0006281	biological_process	DNA repair
K	0006974	biological_process	DNA damage response
K	0046872	molecular_function	metal ion binding
M	0003697	molecular_function	single-stranded DNA binding
M	0006301	biological_process	postreplication repair
M	0006513	biological_process	protein monoubiquitination
M	0061630	molecular_function	ubiquitin protein ligase activity
N	0000122	biological_process	negative regulation of transcription by RNA polymerase II
N	0000151	cellular_component	ubiquitin ligase complex
N	0000209	biological_process	protein polyubiquitination
N	0004842	molecular_function	ubiquitin-protein transferase activity
N	0005515	molecular_function	protein binding
N	0005524	molecular_function	ATP binding
N	0005634	cellular_component	nucleus
N	0005654	cellular_component	nucleoplasm
N	0005768	cellular_component	endosome
N	0005829	cellular_component	cytosol
N	0005886	cellular_component	plasma membrane
N	0006281	biological_process	DNA repair
N	0006511	biological_process	ubiquitin-dependent protein catabolic process
N	0006513	biological_process	protein monoubiquitination
N	0006915	biological_process	apoptotic process
N	0010008	cellular_component	endosome membrane
N	0016567	biological_process	protein ubiquitination
N	0016740	molecular_function	transferase activity
N	0019787	molecular_function	ubiquitin-like protein transferase activity
N	0030514	biological_process	negative regulation of BMP signaling pathway
N	0031625	molecular_function	ubiquitin protein ligase binding
N	0036211	biological_process	protein modification process
N	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
N	0051865	biological_process	protein autoubiquitination
N	0061630	molecular_function	ubiquitin protein ligase activity
N	0061631	molecular_function	ubiquitin conjugating enzyme activity
N	0070062	cellular_component	extracellular exosome
N	0070936	biological_process	protein K48-linked ubiquitination
N	0070979	biological_process	protein K11-linked ubiquitination
N	0085020	biological_process	protein K6-linked ubiquitination
N	1903955	biological_process	positive regulation of protein targeting to mitochondrion

Functional Information from PROSITE/UniProt

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO66-ILE74

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

Chain	Residue	Details
N	TYR74-LEU89

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

Chain	Residue	Details
C	ALA21-VAL27

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

Chain	Residue	Details
D	ARG92-GLY114
D	ARG186-GLY208

site_id	PS00518
Number of Residues	10
Details	ZF_RING_1 Zinc finger RING-type signature. CeHiFCsnCV

Chain	Residue	Details
M	CYS66-VAL75
K	CYS39-MET48

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Glycyl thioester intermediate => ECO:0000255\|PROSITE-ProRule:PRU00388, ECO:0000255\|PROSITE-ProRule:PRU10133

Chain	Residue	Details
N	CYS85
D	LYS116
D	LYS120
H	LYS34
H	LYS116
H	LYS120

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250\|UniProtKB:Q64475

Chain	Residue	Details
G	LYS74
G	LYS75
D	GLU35
H	GLU35

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by AMPK => ECO:0000250\|UniProtKB:Q8CGP1

Chain	Residue	Details
D	SER36
H	SER36

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-lactoyllysine; alternate => ECO:0000269\|PubMed:31645732

Chain	Residue	Details
H	LYS43
H	LYS85
D	LYS43
D	LYS85

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:16627869

Chain	Residue	Details
D	LYS46
D	LYS108
H	LYS46
H	LYS108

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269\|PubMed:24681537

Chain	Residue	Details
D	LYS57
H	LYS57

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Dimethylated arginine => ECO:0000250\|UniProtKB:Q96A08

Chain	Residue	Details
G	LYS119
D	ARG79
H	ARG79

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:Q96A08

Chain	Residue	Details
D	ARG86
D	ARG92
H	ARG86
H	ARG92

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q00729

Chain	Residue	Details
D	THR115
H	THR115

site_id	SWS_FT_FI10
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250\|UniProtKB:P62807

Chain	Residue	Details
D	SER112
F	LYS91
H	SER112

site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:21726816

Chain	Residue	Details
D	LYS34
H	LYS34
F	LYS59
F	LYS79

site_id	SWS_FT_FI12
Number of Residues	4
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
H	LYS120
A	SER110
D	LYS120

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