4EC9
Crystal structure of full-length cdk9 in complex with cyclin t
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 |
| 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 | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| B | SER117 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ILE25 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18566585 |
| Chain | Residue | Details |
| A | LYS48 | |
| A | ASP104 | |
| A | ASP167 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; by EP300/CBP, PCAF/KAT2B and GCN5/KAT2A => ECO:0000269|PubMed:17452463, ECO:0000269|PubMed:18250157 |
| Chain | Residue | Details |
| A | LYS44 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A => ECO:0000269|PubMed:18250157, ECO:0000269|PubMed:28426094 |
| Chain | Residue | Details |
| A | LYS48 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:21533037 |
| Chain | Residue | Details |
| A | SER175 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CaMK1D => ECO:0000269|PubMed:15965233, ECO:0000269|PubMed:18483222, ECO:0000269|PubMed:18566585, ECO:0000269|PubMed:18829461, ECO:0000269|PubMed:20535204, ECO:0000269|PubMed:20851342, ECO:0000269|PubMed:21448926, ECO:0000269|PubMed:21779453, ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | TPO186 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by CDK9 and PKA => ECO:0000269|PubMed:10958691, ECO:0000269|PubMed:18566585, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER347 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CDK9 => ECO:0000269|PubMed:10958691, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | THR350 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by CDK9 => ECO:0000269|PubMed:10958691 |
| Chain | Residue | Details |
| A | SER353 | |
| A | SER357 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CDK9 => ECO:0000269|PubMed:10958691 |
| Chain | Residue | Details |
| A | THR354 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by CDK9 => ECO:0000269|PubMed:18566585 |
| Chain | Residue | Details |
| A | THR362 | |
| A | THR363 |
