9CKC

Crystal structure of SMYD2 in complex with two PARP1 peptides

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000993	molecular_function	RNA polymerase II complex binding
A	0002039	molecular_function	p53 binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006325	biological_process	chromatin organization
A	0006338	biological_process	chromatin remodeling
A	0007507	biological_process	heart development
A	0008168	molecular_function	methyltransferase activity
A	0008270	molecular_function	zinc ion binding
A	0008285	biological_process	negative regulation of cell population proliferation
A	0016278	molecular_function	lysine N-methyltransferase activity
A	0016279	molecular_function	protein-lysine N-methyltransferase activity
A	0016740	molecular_function	transferase activity
A	0018026	biological_process	peptidyl-lysine monomethylation
A	0018027	biological_process	peptidyl-lysine dimethylation
A	0032259	biological_process	methylation
A	0042054	molecular_function	histone methyltransferase activity
A	0043516	biological_process	regulation of DNA damage response, signal transduction by p53 class mediator
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0046872	molecular_function	metal ion binding
A	0046975	molecular_function	histone H3K36 methyltransferase activity
A	0140938	molecular_function	histone H3 methyltransferase activity
A	0140999	molecular_function	histone H3K4 trimethyltransferase activity
A	1901796	biological_process	regulation of signal transduction by p53 class mediator
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0000993	molecular_function	RNA polymerase II complex binding
B	0002039	molecular_function	p53 binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006325	biological_process	chromatin organization
B	0006338	biological_process	chromatin remodeling
B	0007507	biological_process	heart development
B	0008168	molecular_function	methyltransferase activity
B	0008270	molecular_function	zinc ion binding
B	0008285	biological_process	negative regulation of cell population proliferation
B	0016278	molecular_function	lysine N-methyltransferase activity
B	0016279	molecular_function	protein-lysine N-methyltransferase activity
B	0016740	molecular_function	transferase activity
B	0018026	biological_process	peptidyl-lysine monomethylation
B	0018027	biological_process	peptidyl-lysine dimethylation
B	0032259	biological_process	methylation
B	0042054	molecular_function	histone methyltransferase activity
B	0043516	biological_process	regulation of DNA damage response, signal transduction by p53 class mediator
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0046872	molecular_function	metal ion binding
B	0046975	molecular_function	histone H3K36 methyltransferase activity
B	0140938	molecular_function	histone H3 methyltransferase activity
B	0140999	molecular_function	histone H3K4 trimethyltransferase activity
B	1901796	biological_process	regulation of signal transduction by p53 class mediator

Functional Information from PROSITE/UniProt

site_id	PS01360
Number of Residues	40
Details	ZF_MYND_1 Zinc finger MYND-type signature. Hcey.Cftrkeglsk........CgrCkqafYCnveCqkedwpm..Hkle.C

Chain	Residue	Details
A	HIS51-CYS90

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	468
Details	Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	76
Details	Zinc finger: {"description":"MYND-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21724641","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---