4EC9
Crystal structure of full-length cdk9 in complex with cyclin t
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000976 | molecular_function | transcription cis-regulatory region binding |
A | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
A | 0001223 | molecular_function | transcription coactivator binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003682 | molecular_function | chromatin binding |
A | 0003711 | molecular_function | transcription elongation factor activity |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004693 | molecular_function | cyclin-dependent protein serine/threonine kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0006281 | biological_process | DNA repair |
A | 0006282 | biological_process | regulation of DNA repair |
A | 0006366 | biological_process | transcription by RNA polymerase II |
A | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
A | 0006368 | biological_process | transcription elongation by RNA polymerase II |
A | 0006468 | biological_process | protein phosphorylation |
A | 0006974 | biological_process | DNA damage response |
A | 0007346 | biological_process | regulation of mitotic cell cycle |
A | 0008023 | cellular_component | transcription elongation factor complex |
A | 0008024 | cellular_component | cyclin/CDK positive transcription elongation factor complex |
A | 0008283 | biological_process | cell population proliferation |
A | 0008353 | molecular_function | RNA polymerase II CTD heptapeptide repeat kinase activity |
A | 0016020 | cellular_component | membrane |
A | 0016301 | molecular_function | kinase activity |
A | 0016605 | cellular_component | PML body |
A | 0016740 | molecular_function | transferase activity |
A | 0017069 | molecular_function | snRNA binding |
A | 0019901 | molecular_function | protein kinase binding |
A | 0031297 | biological_process | replication fork processing |
A | 0031440 | biological_process | regulation of mRNA 3'-end processing |
A | 0032968 | biological_process | positive regulation of transcription elongation by RNA polymerase II |
A | 0034244 | biological_process | negative regulation of transcription elongation by RNA polymerase II |
A | 0036464 | cellular_component | cytoplasmic ribonucleoprotein granule |
A | 0043923 | biological_process | positive regulation by host of viral transcription |
A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
A | 0051147 | biological_process | regulation of muscle cell differentiation |
A | 0051647 | biological_process | nucleus localization |
A | 0051726 | biological_process | regulation of cell cycle |
A | 0070691 | cellular_component | P-TEFb complex |
A | 0071345 | biological_process | cellular response to cytokine stimulus |
A | 0097322 | molecular_function | 7SK snRNA binding |
A | 0106310 | molecular_function | protein serine kinase activity |
A | 0120186 | biological_process | negative regulation of protein localization to chromatin |
A | 0120187 | biological_process | positive regulation of protein localization to chromatin |
A | 0140673 | biological_process | transcription elongation-coupled chromatin remodeling |
A | 0160239 | biological_process | transcription pausing by RNA polymerase II |
B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
B | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGTFGEVFkArhrktgqk..........VALK |
Chain | Residue | Details |
A | ILE25-LYS48 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDMKaaNVLI |
Chain | Residue | Details |
A | ILE145-ILE157 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18566585","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine; by EP300/CBP, PCAF/KAT2B and GCN5/KAT2A","evidences":[{"source":"PubMed","id":"17452463","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18250157","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A","evidences":[{"source":"PubMed","id":"18250157","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28426094","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21533037","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by CaMK1D","evidences":[{"source":"PubMed","id":"15965233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18483222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18566585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18829461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20535204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20851342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21448926","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21779453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |