Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6X0M

Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin

Functional Information from GO Data

Chain	GOid	namespace	contents
o	0000785	cellular_component	chromatin
o	0003682	molecular_function	chromatin binding
o	0005515	molecular_function	protein binding
o	0005634	cellular_component	nucleus
o	0005694	cellular_component	chromosome
o	0006281	biological_process	DNA repair
o	0006302	biological_process	double-strand break repair
o	0006974	biological_process	DNA damage response
o	0010835	biological_process	regulation of protein ADP-ribosylation
o	0042393	molecular_function	histone binding
o	0072572	molecular_function	poly-ADP-D-ribose binding
o	0090734	cellular_component	site of DNA damage
o	0140768	molecular_function	protein ADP-ribosyltransferase-substrate adaptor activity
o	0140861	biological_process	DNA repair-dependent chromatin remodeling
O	0000785	cellular_component	chromatin
O	0003682	molecular_function	chromatin binding
O	0005515	molecular_function	protein binding
O	0005634	cellular_component	nucleus
O	0005694	cellular_component	chromosome
O	0006281	biological_process	DNA repair
O	0006302	biological_process	double-strand break repair
O	0006974	biological_process	DNA damage response
O	0010835	biological_process	regulation of protein ADP-ribosylation
O	0042393	molecular_function	histone binding
O	0072572	molecular_function	poly-ADP-D-ribose binding
O	0090734	cellular_component	site of DNA damage
O	0140768	molecular_function	protein ADP-ribosyltransferase-substrate adaptor activity
O	0140861	biological_process	DNA repair-dependent chromatin remodeling
p	0003677	molecular_function	DNA binding
p	0003682	molecular_function	chromatin binding
p	0003684	molecular_function	damaged DNA binding
p	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity
p	0005515	molecular_function	protein binding
p	0005634	cellular_component	nucleus
p	0005654	cellular_component	nucleoplasm
p	0005694	cellular_component	chromosome
p	0005730	cellular_component	nucleolus
p	0006281	biological_process	DNA repair
p	0006284	biological_process	base-excision repair
p	0006302	biological_process	double-strand break repair
p	0006974	biological_process	DNA damage response
p	0016757	molecular_function	glycosyltransferase activity
p	0016779	molecular_function	nucleotidyltransferase activity
p	0030592	biological_process	DNA ADP-ribosylation
p	0031491	molecular_function	nucleosome binding
p	0046697	biological_process	decidualization
p	0061051	biological_process	positive regulation of cell growth involved in cardiac muscle cell development
p	0070212	biological_process	protein poly-ADP-ribosylation
p	0070213	biological_process	protein auto-ADP-ribosylation
p	0072572	molecular_function	poly-ADP-D-ribose binding
p	0090649	biological_process	response to oxygen-glucose deprivation
p	0090734	cellular_component	site of DNA damage
p	0097191	biological_process	extrinsic apoptotic signaling pathway
p	0110088	biological_process	hippocampal neuron apoptotic process
p	0140294	molecular_function	NAD DNA ADP-ribosyltransferase activity
p	0140805	molecular_function	NAD+-protein-serine ADP-ribosyltransferase activity
p	0140806	molecular_function	NAD+- protein-aspartate ADP-ribosyltransferase activity
p	0140807	molecular_function	NAD+-protein-glutamate ADP-ribosyltransferase activity
p	0140861	biological_process	DNA repair-dependent chromatin remodeling
p	0160004	molecular_function	poly-ADP-D-ribose modification-dependent protein binding
p	1990404	molecular_function	NAD+-protein ADP-ribosyltransferase activity
P	0003677	molecular_function	DNA binding
P	0003682	molecular_function	chromatin binding
P	0003684	molecular_function	damaged DNA binding
P	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity
P	0005515	molecular_function	protein binding
P	0005634	cellular_component	nucleus
P	0005654	cellular_component	nucleoplasm
P	0005694	cellular_component	chromosome
P	0005730	cellular_component	nucleolus
P	0006281	biological_process	DNA repair
P	0006284	biological_process	base-excision repair
P	0006302	biological_process	double-strand break repair
P	0006974	biological_process	DNA damage response
P	0016757	molecular_function	glycosyltransferase activity
P	0016779	molecular_function	nucleotidyltransferase activity
P	0030592	biological_process	DNA ADP-ribosylation
P	0031491	molecular_function	nucleosome binding
P	0046697	biological_process	decidualization
P	0061051	biological_process	positive regulation of cell growth involved in cardiac muscle cell development
P	0070212	biological_process	protein poly-ADP-ribosylation
P	0070213	biological_process	protein auto-ADP-ribosylation
P	0072572	molecular_function	poly-ADP-D-ribose binding
P	0090649	biological_process	response to oxygen-glucose deprivation
P	0090734	cellular_component	site of DNA damage
P	0097191	biological_process	extrinsic apoptotic signaling pathway
P	0110088	biological_process	hippocampal neuron apoptotic process
P	0140294	molecular_function	NAD DNA ADP-ribosyltransferase activity
P	0140805	molecular_function	NAD+-protein-serine ADP-ribosyltransferase activity
P	0140806	molecular_function	NAD+- protein-aspartate ADP-ribosyltransferase activity
P	0140807	molecular_function	NAD+-protein-glutamate ADP-ribosyltransferase activity
P	0140861	biological_process	DNA repair-dependent chromatin remodeling
P	0160004	molecular_function	poly-ADP-D-ribose modification-dependent protein binding
P	1990404	molecular_function	NAD+-protein ADP-ribosyltransferase activity

Functional Information from PROSITE/UniProt

site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLEANPKA

Chain	Residue	Details
P	LEU485-ALA492

site_id	PS01121
Number of Residues	15
Details	CASPASE_HIS Caspase family histidine active site. HgsrmSnwVgILSHG

Chain	Residue	Details
P	HIS415-GLY429

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: For poly [ADP-ribose] polymerase activity => ECO:0000305\|PubMed:26704974, ECO:0000305\|PubMed:30104678, ECO:0000305\|PubMed:32028527

Chain	Residue	Details
P	TYR558
p	TYR558

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:32028527, ECO:0007744\|PDB:6TX3

Chain	Residue	Details
P	HIS428
P	ALA437
P	PHE444
P	GLY470
p	HIS428
p	ALA437
p	PHE444
p	GLY470

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Cleavage; by caspase-8 => ECO:0000250\|UniProtKB:O88554

Chain	Residue	Details
P	LYS207
p	LYS207

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:O88554

Chain	Residue	Details
P	LYS37
P	LYS38
p	LYS37
p	LYS38

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:21406692

Chain	Residue	Details
P	GLN226
P	ILE232
p	GLN226
p	ILE232

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269\|PubMed:33589610

Chain	Residue	Details
O	ASP235
o	ASP235

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: ADP-ribosyltyrosine => ECO:0000269\|PubMed:29954836, ECO:0000269\|PubMed:30257210

Chain	Residue	Details
O	TYR238
o	TYR238

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269\|PubMed:33589610

Chain	Residue	Details
O	GLU240
o	GLU240

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