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	0003824	molecular_function	catalytic activity
p	0003950	molecular_function	NAD+ poly-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	0006302	biological_process	double-strand break repair
p	0006974	biological_process	DNA damage response
p	0016740	molecular_function	transferase activity
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	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	0090734	cellular_component	site of DNA damage
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 mono-ADP-ribosyltransferase activity
P	0003677	molecular_function	DNA binding
P	0003682	molecular_function	chromatin binding
P	0003684	molecular_function	damaged DNA binding
P	0003824	molecular_function	catalytic activity
P	0003950	molecular_function	NAD+ poly-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	0006302	biological_process	double-strand break repair
P	0006974	biological_process	DNA damage response
P	0016740	molecular_function	transferase activity
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	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	0090734	cellular_component	site of DNA damage
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 mono-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	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33683197","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"PolyADP-ribosyl aspartic acid","evidences":[{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosyltyrosine","evidences":[{"source":"PubMed","id":"29954836","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30257210","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	194
Details	Domain: {"description":"WGR","evidences":[{"source":"PROSITE-ProRule","id":"PRU01321","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	454
Details	Domain: {"description":"PARP catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00397","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Active site: {"description":"For poly [ADP-ribose] polymerase activity","evidences":[{"source":"PubMed","id":"26704974","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"30104678","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TX3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Site: {"description":"Cleavage; by caspase-8","evidences":[{"source":"UniProtKB","id":"O88554","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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