8QW9
RNAPII elongation complex bound to RECQ5_R502E
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| A | 0000791 | cellular_component | euchromatin |
| A | 0001046 | molecular_function | core promoter sequence-specific DNA binding |
| A | 0001172 | biological_process | RNA-templated transcription |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| A | 0003968 | molecular_function | RNA-directed RNA polymerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005665 | cellular_component | RNA polymerase II, core complex |
| A | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042789 | biological_process | mRNA transcription by RNA polymerase II |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071667 | molecular_function | DNA/RNA hybrid binding |
| B | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| B | 0000781 | cellular_component | chromosome, telomeric region |
| B | 0001172 | biological_process | RNA-templated transcription |
| B | 0003682 | molecular_function | chromatin binding |
| B | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| B | 0003968 | molecular_function | RNA-directed RNA polymerase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005665 | cellular_component | RNA polymerase II, core complex |
| B | 0006366 | biological_process | transcription by RNA polymerase II |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071667 | molecular_function | DNA/RNA hybrid binding |
| C | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| C | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005665 | cellular_component | RNA polymerase II, core complex |
| C | 0005829 | cellular_component | cytosol |
| C | 0006366 | biological_process | transcription by RNA polymerase II |
| C | 0008270 | molecular_function | zinc ion binding |
| D | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| D | 0005634 | cellular_component | nucleus |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005665 | cellular_component | RNA polymerase II, core complex |
| D | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
| D | 0031369 | molecular_function | translation initiation factor binding |
| E | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| E | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005654 | cellular_component | nucleoplasm |
| E | 0005665 | cellular_component | RNA polymerase II, core complex |
| E | 0005666 | cellular_component | RNA polymerase III complex |
| E | 0005730 | cellular_component | nucleolus |
| E | 0005736 | cellular_component | RNA polymerase I complex |
| E | 0006362 | biological_process | transcription elongation by RNA polymerase I |
| E | 0006366 | biological_process | transcription by RNA polymerase II |
| E | 0042797 | biological_process | tRNA transcription by RNA polymerase III |
| F | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| F | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| F | 0005634 | cellular_component | nucleus |
| F | 0005665 | cellular_component | RNA polymerase II, core complex |
| F | 0005666 | cellular_component | RNA polymerase III complex |
| F | 0005730 | cellular_component | nucleolus |
| F | 0005736 | cellular_component | RNA polymerase I complex |
| F | 0006360 | biological_process | transcription by RNA polymerase I |
| F | 0006366 | biological_process | transcription by RNA polymerase II |
| F | 0042797 | biological_process | tRNA transcription by RNA polymerase III |
| G | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| G | 0000932 | cellular_component | P-body |
| G | 0000956 | biological_process | nuclear-transcribed mRNA catabolic process |
| G | 0003697 | molecular_function | single-stranded DNA binding |
| G | 0003723 | molecular_function | RNA binding |
| G | 0003727 | molecular_function | single-stranded RNA binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005665 | cellular_component | RNA polymerase II, core complex |
| G | 0006366 | biological_process | transcription by RNA polymerase II |
| G | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
| G | 0031369 | molecular_function | translation initiation factor binding |
| G | 0045948 | biological_process | positive regulation of translational initiation |
| G | 0060213 | biological_process | positive regulation of nuclear-transcribed mRNA poly(A) tail shortening |
| H | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| H | 0003697 | molecular_function | single-stranded DNA binding |
| H | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| H | 0005634 | cellular_component | nucleus |
| H | 0005654 | cellular_component | nucleoplasm |
| H | 0005665 | cellular_component | RNA polymerase II, core complex |
| H | 0005666 | cellular_component | RNA polymerase III complex |
| H | 0005730 | cellular_component | nucleolus |
| H | 0005736 | cellular_component | RNA polymerase I complex |
| H | 0006366 | biological_process | transcription by RNA polymerase II |
| H | 0032993 | cellular_component | protein-DNA complex |
| I | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| I | 0001193 | biological_process | maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II |
| I | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| I | 0005634 | cellular_component | nucleus |
| I | 0005654 | cellular_component | nucleoplasm |
| I | 0005665 | cellular_component | RNA polymerase II, core complex |
| I | 0005730 | cellular_component | nucleolus |
| I | 0006283 | biological_process | transcription-coupled nucleotide-excision repair |
| I | 0006366 | biological_process | transcription by RNA polymerase II |
| I | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
| I | 0008270 | molecular_function | zinc ion binding |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| J | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| J | 0005634 | cellular_component | nucleus |
| J | 0005654 | cellular_component | nucleoplasm |
| J | 0005665 | cellular_component | RNA polymerase II, core complex |
| J | 0005666 | cellular_component | RNA polymerase III complex |
| J | 0005730 | cellular_component | nucleolus |
| J | 0005736 | cellular_component | RNA polymerase I complex |
| J | 0006360 | biological_process | transcription by RNA polymerase I |
| J | 0006366 | biological_process | transcription by RNA polymerase II |
| J | 0008270 | molecular_function | zinc ion binding |
| J | 0042797 | biological_process | tRNA transcription by RNA polymerase III |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| K | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| K | 0005634 | cellular_component | nucleus |
| K | 0005665 | cellular_component | RNA polymerase II, core complex |
| K | 0006366 | biological_process | transcription by RNA polymerase II |
| L | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| L | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| L | 0005634 | cellular_component | nucleus |
| L | 0005654 | cellular_component | nucleoplasm |
| L | 0005665 | cellular_component | RNA polymerase II, core complex |
| L | 0005666 | cellular_component | RNA polymerase III complex |
| L | 0005730 | cellular_component | nucleolus |
| L | 0005736 | cellular_component | RNA polymerase I complex |
| L | 0006366 | biological_process | transcription by RNA polymerase II |
| L | 0008270 | molecular_function | zinc ion binding |
| L | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DNDPNDYVEqdDI |
| Chain | Residue | Details |
| C | ASP136-ILE148 |
| site_id | PS00115 |
| Number of Residues | 7 |
| Details | RNA_POL_II_REPEAT Eukaryotic RNA polymerase II heptapeptide repeat. YSPTSPA |
| Chain | Residue | Details |
| A | TYR1593-ALA1599 | |
| A | TYR1671-SER1677 | |
| A | TYR1678-SER1684 | |
| A | TYR1685-SER1691 | |
| A | TYR1692-SER1698 | |
| A | TYR1699-SER1705 | |
| A | TYR1706-SER1712 | |
| A | TYR1713-SER1719 | |
| A | TYR1720-SER1726 | |
| A | TYR1727-SER1733 | |
| A | TYR1734-SER1740 | |
| A | TYR1615-SER1621 | |
| A | TYR1741-ASN1747 | |
| A | TYR1748-ASN1754 | |
| A | TYR1755-SER1761 | |
| A | TYR1762-SER1768 | |
| A | TYR1769-ASN1775 | |
| A | TYR1776-ASN1782 | |
| A | TYR1783-SER1789 | |
| A | TYR1790-SER1796 | |
| A | TYR1797-SER1803 | |
| A | TYR1818-SER1824 | |
| A | TYR1622-SER1628 | |
| A | TYR1825-SER1831 | |
| A | TYR1832-LYS1838 | |
| A | TYR1839-SER1845 | |
| A | TYR1853-LYS1859 | |
| A | TYR1860-LYS1866 | |
| A | TYR1867-LYS1873 | |
| A | TYR1874-THR1880 | |
| A | TYR1888-THR1894 | |
| A | TYR1902-LYS1908 | |
| A | TYR1909-THR1915 | |
| A | TYR1629-ASN1635 | |
| A | TYR1916-LYS1922 | |
| A | TYR1923-THR1929 | |
| A | TYR1930-LYS1936 | |
| A | TYR1947-THR1953 | |
| A | TYR1636-SER1642 | |
| A | TYR1643-SER1649 | |
| A | TYR1650-SER1656 | |
| A | TYR1657-SER1663 | |
| A | TYR1664-SER1670 |
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YVCTAPH |
| Chain | Residue | Details |
| I | TYR112-HIS118 |
| site_id | PS00446 |
| Number of Residues | 41 |
| Details | RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NSIRRvfiaevpiiAidwVqidaNsSvlhDEfIAhRLGLIP |
| Chain | Residue | Details |
| C | ASN32-PRO72 |
| site_id | PS00466 |
| Number of Residues | 38 |
| Details | ZF_TFIIS_1 Zinc finger TFIIS-type signature. CqkCghkeavffqSHSARaEDAmrlyyvCtaph.CghrW |
| Chain | Residue | Details |
| I | CYS86-TRP123 |
| site_id | PS00690 |
| Number of Residues | 10 |
| Details | DEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. SyLVVDEAHC |
| Chain | Residue | Details |
| R | SER152-CYS161 |
| site_id | PS01030 |
| Number of Residues | 27 |
| Details | RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCQECNNMLypkedkenrillyaCrnC |
| Chain | Residue | Details |
| I | PHE16-CYS42 |
| site_id | PS01110 |
| Number of Residues | 14 |
| Details | RNA_POL_H_23KD RNA polymerases H / 23 Kd subunits signature. HELVPEHvvMtkEE |
| Chain | Residue | Details |
| E | HIS142-GLU155 |
| site_id | PS01111 |
| Number of Residues | 15 |
| Details | RNA_POL_K_14KD RNA polymerases K / 14 to 18 Kd subunits signature. TkYErARvLGtRAlQ |
| Chain | Residue | Details |
| F | THR58-GLN72 |
| site_id | PS01112 |
| Number of Residues | 10 |
| Details | RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IIPVrCFTCG |
| Chain | Residue | Details |
| J | ILE2-GLY11 |
| site_id | PS01154 |
| Number of Residues | 32 |
| Details | RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. InkEdHTLgNiIksqLlkdpqVlfagYkvpHP |
| Chain | Residue | Details |
| K | ILE35-PRO66 |
| site_id | PS01166 |
| Number of Residues | 13 |
| Details | RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT |
| Chain | Residue | Details |
| B | GLY932-THR944 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 41 |
| Details | Region: {"description":"Bridging helix","evidences":[{"source":"PubMed","id":"26789250","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26789250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FLM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26789250","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28892040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FLM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OIK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28892040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OIK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P24928","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P04050","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24928","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 41 |
| Details | Zinc finger: {"description":"C4-type","evidences":[{"source":"PubMed","id":"26789250","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28892040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FLM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OIK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P30876","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P08518","evidenceCode":"ECO:0000250"},{"source":"UniProtKB","id":"P30876","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P30876","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P30876","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 23 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19387","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P19388","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P52434","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 25 |
| Details | Zinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 42 |
| Details | Zinc finger: {"description":"TFIIS-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00472","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10145","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26789250","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28892040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FLM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OIK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00472","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26789250","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28892040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FLM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OIK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00472","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26789250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FLM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P52435","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






