9CKG
Crystal structure of SMYD2 active site mutant
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 | 0006338 | biological_process | chromatin remodeling |
| A | 0007507 | biological_process | heart development |
| 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 | 0018026 | biological_process | peptidyl-lysine monomethylation |
| A | 0018027 | biological_process | peptidyl-lysine dimethylation |
| 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 | 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 |
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 | 234 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 38 |
| 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 | 5 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
