Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7JZV

Cryo-EM structure of the BRCA1-UbcH5c/BARD1 E3-E2 module bound to a nucleosome

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	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	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	0046872	molecular_function	metal ion binding
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
B	0003697	molecular_function	single-stranded DNA binding
B	0006301	biological_process	postreplication repair
B	0006513	biological_process	protein monoubiquitination
B	0061630	molecular_function	ubiquitin protein ligase activity
N	0000786	cellular_component	nucleosome
N	0003674	molecular_function	molecular_function
N	0003677	molecular_function	DNA binding
N	0005515	molecular_function	protein binding
N	0005634	cellular_component	nucleus
N	0005694	cellular_component	chromosome
N	0008150	biological_process	biological_process
N	0030527	molecular_function	structural constituent of chromatin
N	0031492	molecular_function	nucleosomal DNA binding
N	0031507	biological_process	heterochromatin formation
N	0043229	cellular_component	intracellular organelle
N	0046982	molecular_function	protein heterodimerization activity
N	0070062	cellular_component	extracellular exosome
O	0000786	cellular_component	nucleosome
O	0002227	biological_process	innate immune response in mucosa
O	0003674	molecular_function	molecular_function
O	0003677	molecular_function	DNA binding
O	0005515	molecular_function	protein binding
O	0005615	cellular_component	extracellular space
O	0005634	cellular_component	nucleus
O	0005654	cellular_component	nucleoplasm
O	0005694	cellular_component	chromosome
O	0005829	cellular_component	cytosol
O	0019731	biological_process	antibacterial humoral response
O	0030527	molecular_function	structural constituent of chromatin
O	0031640	biological_process	killing of cells of another organism
O	0042742	biological_process	defense response to bacterium
O	0043229	cellular_component	intracellular organelle
O	0046982	molecular_function	protein heterodimerization activity
O	0050829	biological_process	defense response to Gram-negative bacterium
O	0050830	biological_process	defense response to Gram-positive bacterium
O	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
P	0000786	cellular_component	nucleosome
P	0003677	molecular_function	DNA binding
P	0005515	molecular_function	protein binding
P	0005576	cellular_component	extracellular region
P	0005634	cellular_component	nucleus
P	0005654	cellular_component	nucleoplasm
P	0005694	cellular_component	chromosome
P	0006325	biological_process	chromatin organization
P	0006334	biological_process	nucleosome assembly
P	0030527	molecular_function	structural constituent of chromatin
P	0043229	cellular_component	intracellular organelle
P	0046982	molecular_function	protein heterodimerization activity
P	0070062	cellular_component	extracellular exosome
Q	0000781	cellular_component	chromosome, telomeric region
Q	0000786	cellular_component	nucleosome
Q	0003677	molecular_function	DNA binding
Q	0003723	molecular_function	RNA binding
Q	0005515	molecular_function	protein binding
Q	0005576	cellular_component	extracellular region
Q	0005634	cellular_component	nucleus
Q	0005654	cellular_component	nucleoplasm
Q	0005694	cellular_component	chromosome
Q	0006325	biological_process	chromatin organization
Q	0006334	biological_process	nucleosome assembly
Q	0016020	cellular_component	membrane
Q	0030527	molecular_function	structural constituent of chromatin
Q	0032200	biological_process	telomere organization
Q	0032991	cellular_component	protein-containing complex
Q	0043505	cellular_component	CENP-A containing nucleosome
Q	0045653	biological_process	negative regulation of megakaryocyte differentiation
Q	0046982	molecular_function	protein heterodimerization activity
Q	0061644	biological_process	protein localization to CENP-A containing chromatin
Q	0070062	cellular_component	extracellular exosome
n	0000786	cellular_component	nucleosome
n	0003674	molecular_function	molecular_function
n	0003677	molecular_function	DNA binding
n	0005515	molecular_function	protein binding
n	0005634	cellular_component	nucleus
n	0005694	cellular_component	chromosome
n	0008150	biological_process	biological_process
n	0030527	molecular_function	structural constituent of chromatin
n	0031492	molecular_function	nucleosomal DNA binding
n	0031507	biological_process	heterochromatin formation
n	0043229	cellular_component	intracellular organelle
n	0046982	molecular_function	protein heterodimerization activity
n	0070062	cellular_component	extracellular exosome
o	0000786	cellular_component	nucleosome
o	0002227	biological_process	innate immune response in mucosa
o	0003674	molecular_function	molecular_function
o	0003677	molecular_function	DNA binding
o	0005515	molecular_function	protein binding
o	0005615	cellular_component	extracellular space
o	0005634	cellular_component	nucleus
o	0005654	cellular_component	nucleoplasm
o	0005694	cellular_component	chromosome
o	0005829	cellular_component	cytosol
o	0019731	biological_process	antibacterial humoral response
o	0030527	molecular_function	structural constituent of chromatin
o	0031640	biological_process	killing of cells of another organism
o	0042742	biological_process	defense response to bacterium
o	0043229	cellular_component	intracellular organelle
o	0046982	molecular_function	protein heterodimerization activity
o	0050829	biological_process	defense response to Gram-negative bacterium
o	0050830	biological_process	defense response to Gram-positive bacterium
o	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
p	0000786	cellular_component	nucleosome
p	0003677	molecular_function	DNA binding
p	0005515	molecular_function	protein binding
p	0005576	cellular_component	extracellular region
p	0005634	cellular_component	nucleus
p	0005654	cellular_component	nucleoplasm
p	0005694	cellular_component	chromosome
p	0006325	biological_process	chromatin organization
p	0006334	biological_process	nucleosome assembly
p	0030527	molecular_function	structural constituent of chromatin
p	0043229	cellular_component	intracellular organelle
p	0046982	molecular_function	protein heterodimerization activity
p	0070062	cellular_component	extracellular exosome
q	0000781	cellular_component	chromosome, telomeric region
q	0000786	cellular_component	nucleosome
q	0003677	molecular_function	DNA binding
q	0003723	molecular_function	RNA binding
q	0005515	molecular_function	protein binding
q	0005576	cellular_component	extracellular region
q	0005634	cellular_component	nucleus
q	0005654	cellular_component	nucleoplasm
q	0005694	cellular_component	chromosome
q	0006325	biological_process	chromatin organization
q	0006334	biological_process	nucleosome assembly
q	0016020	cellular_component	membrane
q	0030527	molecular_function	structural constituent of chromatin
q	0032200	biological_process	telomere organization
q	0032991	cellular_component	protein-containing complex
q	0043505	cellular_component	CENP-A containing nucleosome
q	0045653	biological_process	negative regulation of megakaryocyte differentiation
q	0046982	molecular_function	protein heterodimerization activity
q	0061644	biological_process	protein localization to CENP-A containing chromatin
q	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
N	ALA21-VAL27

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
Q	GLY14-HIS18

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

Chain	Residue	Details
O	ARG92-GLY114

site_id	PS00322
Number of Residues	7
Details	HISTONE_H3_1 Histone H3 signature 1. KAPRKQL

Chain	Residue	Details
P	LYS14-LEU20

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

Chain	Residue	Details
P	PRO66-ILE74

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

Chain	Residue	Details
A	CYS39-MET48
B	CYS66-VAL75

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Citrulline; alternate => ECO:0000269\|PubMed:16567635

Chain	Residue	Details
P	ARG2
p	ARG2

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by HASPIN => ECO:0000269\|PubMed:15681610, ECO:0000269\|PubMed:16185088

Chain	Residue	Details
P	THR3
p	THR3

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:16267050, ECO:0000269\|PubMed:17194708

Chain	Residue	Details
O	LYS43
O	LYS85
o	LYS5
o	LYS11
o	LYS15
o	LYS16
o	LYS20
o	LYS23
o	LYS43
o	LYS85
P	LYS64
p	LYS4
p	LYS18
p	LYS64
P	LYS4
P	LYS18

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269\|PubMed:30867594

Chain	Residue	Details
n	LYS9
n	LYS95
P	GLN5
p	GLN5

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PKC => ECO:0000269\|PubMed:20228790

Chain	Residue	Details
q	LYS8
q	LYS16
q	LYS44
P	THR6
p	THR6
Q	LYS44

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250\|UniProtKB:P84228

Chain	Residue	Details
q	LYS31
q	LYS77
q	LYS91
P	ARG8
p	ARG8
Q	LYS77
Q	LYS91
q	LYS12

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:11242053, ECO:0000269\|PubMed:16185088, ECO:0000269\|PubMed:16267050, ECO:0000269\|PubMed:17194708

Chain	Residue	Details
n	LYS74
n	LYS75
P	LYS9
p	LYS9

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269\|PubMed:10464286, ECO:0000269\|PubMed:11856369, ECO:0000269\|PubMed:12560483, ECO:0000269\|PubMed:15681610, ECO:0000269\|PubMed:16185088

Chain	Residue	Details
o	LYS116
o	LYS120
P	SER10
p	SER10
O	LYS120
o	LYS34

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PKC => ECO:0000269\|PubMed:12560483, ECO:0000269\|PubMed:18066052, ECO:0000269\|PubMed:22901803

Chain	Residue	Details
P	THR11
p	THR11

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435

Chain	Residue	Details
n	LYS119
n	LYS125
p	LYS56
P	LYS14
P	LYS56
p	LYS14

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Citrulline; alternate => ECO:0000269\|PubMed:15345777, ECO:0000269\|PubMed:16497732, ECO:0000269\|PubMed:16567635

Chain	Residue	Details
o	LYS46
o	LYS108
P	ARG17
p	ARG17

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:17194708

Chain	Residue	Details
P	LYS23
p	LYS23

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Citrulline => ECO:0000269\|PubMed:16567635

Chain	Residue	Details
n	LYS119
P	ARG26
p	ARG26

site_id	SWS_FT_FI14
Number of Residues	4
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:16185088, ECO:0000269\|PubMed:16267050, ECO:0000269\|PubMed:16627869, ECO:0000269\|PubMed:17194708

Chain	Residue	Details
p	LYS27
p	LYS36
P	LYS27
P	LYS36

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000269\|PubMed:10464286, ECO:0000269\|PubMed:11856369, ECO:0000269\|PubMed:15681610, ECO:0000269\|PubMed:15684425, ECO:0000269\|PubMed:16185088

Chain	Residue	Details
q	LYS91
P	SER28
p	SER28

site_id	SWS_FT_FI16
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0000250\|UniProtKB:P68431

Chain	Residue	Details
Q	LYS79
q	LYS20
q	LYS59
q	LYS79
p	LYS37
P	LYS37

site_id	SWS_FT_FI17
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269\|PubMed:19783980

Chain	Residue	Details
P	TYR41
p	TYR41

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:20850016

Chain	Residue	Details
o	LYS120
P	SER57
p	SER57

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435, ECO:0000269\|PubMed:29211711

Chain	Residue	Details
P	LYS79
p	LYS79

site_id	SWS_FT_FI20
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:20850016

Chain	Residue	Details
P	THR80
p	THR80

site_id	SWS_FT_FI21
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P84243

Chain	Residue	Details
P	SER86
p	SER86

site_id	SWS_FT_FI22
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:19690332

Chain	Residue	Details
P	THR107
p	THR107

site_id	SWS_FT_FI23
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
P	LYS115
p	LYS115

site_id	SWS_FT_FI24
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435, ECO:0000269\|PubMed:27436229

Chain	Residue	Details
P	LYS122
p	LYS122

site_id	SWS_FT_FI25
Number of Residues	2
Details	LIPID: N6-decanoyllysine => ECO:0000269\|PubMed:35939806

Chain	Residue	Details
P	LYS18
p	LYS18

site_id	SWS_FT_FI26
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000269\|PubMed:21076176

Chain	Residue	Details
P	ALA110
p	ALA110

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