6VEN
Yeast COMPASS in complex with a ubiquitinated nucleosome
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000786 | cellular_component | nucleosome |
| A | 0003677 | molecular_function | DNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005694 | cellular_component | chromosome |
| A | 0030527 | molecular_function | structural constituent of chromatin |
| A | 0031492 | molecular_function | nucleosomal DNA binding |
| A | 0031507 | biological_process | heterochromatin formation |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0000786 | cellular_component | nucleosome |
| B | 0003677 | molecular_function | DNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005694 | cellular_component | chromosome |
| B | 0006334 | biological_process | nucleosome assembly |
| B | 0030527 | molecular_function | structural constituent of chromatin |
| B | 0031507 | biological_process | heterochromatin formation |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0000786 | cellular_component | nucleosome |
| C | 0003677 | molecular_function | DNA binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005694 | cellular_component | chromosome |
| C | 0030527 | molecular_function | structural constituent of chromatin |
| C | 0031507 | biological_process | heterochromatin formation |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0000786 | cellular_component | nucleosome |
| D | 0002227 | biological_process | innate immune response in mucosa |
| D | 0003677 | molecular_function | DNA binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005634 | cellular_component | nucleus |
| D | 0005694 | cellular_component | chromosome |
| D | 0006325 | biological_process | chromatin organization |
| D | 0019731 | biological_process | antibacterial humoral response |
| D | 0030527 | molecular_function | structural constituent of chromatin |
| D | 0031507 | biological_process | heterochromatin formation |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
| E | 0000786 | cellular_component | nucleosome |
| E | 0003677 | molecular_function | DNA binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005654 | cellular_component | nucleoplasm |
| E | 0005694 | cellular_component | chromosome |
| E | 0030527 | molecular_function | structural constituent of chromatin |
| E | 0031492 | molecular_function | nucleosomal DNA binding |
| E | 0031507 | biological_process | heterochromatin formation |
| E | 0046982 | molecular_function | protein heterodimerization activity |
| F | 0000786 | cellular_component | nucleosome |
| F | 0003677 | molecular_function | DNA binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005694 | cellular_component | chromosome |
| F | 0006334 | biological_process | nucleosome assembly |
| F | 0030527 | molecular_function | structural constituent of chromatin |
| F | 0031507 | biological_process | heterochromatin formation |
| F | 0046982 | molecular_function | protein heterodimerization activity |
| G | 0000786 | cellular_component | nucleosome |
| G | 0003677 | molecular_function | DNA binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005694 | cellular_component | chromosome |
| G | 0030527 | molecular_function | structural constituent of chromatin |
| G | 0031507 | biological_process | heterochromatin formation |
| G | 0046982 | molecular_function | protein heterodimerization activity |
| H | 0000786 | cellular_component | nucleosome |
| H | 0002227 | biological_process | innate immune response in mucosa |
| H | 0003677 | molecular_function | DNA binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005615 | cellular_component | extracellular space |
| H | 0005634 | cellular_component | nucleus |
| H | 0005694 | cellular_component | chromosome |
| H | 0006325 | biological_process | chromatin organization |
| H | 0019731 | biological_process | antibacterial humoral response |
| H | 0030527 | molecular_function | structural constituent of chromatin |
| H | 0031507 | biological_process | heterochromatin formation |
| H | 0046982 | molecular_function | protein heterodimerization activity |
| H | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
| L | 0000723 | biological_process | telomere maintenance |
| L | 0000781 | cellular_component | chromosome, telomeric region |
| L | 0005515 | molecular_function | protein binding |
| L | 0005634 | cellular_component | nucleus |
| L | 0031509 | biological_process | subtelomeric heterochromatin formation |
| L | 0042393 | molecular_function | histone binding |
| L | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
| L | 0048188 | cellular_component | Set1C/COMPASS complex |
| L | 1903341 | biological_process | regulation of meiotic DNA double-strand break formation |
| L | 1990234 | cellular_component | transferase complex |
| M | 0000723 | biological_process | telomere maintenance |
| M | 0000781 | cellular_component | chromosome, telomeric region |
| M | 0005515 | molecular_function | protein binding |
| M | 0005634 | cellular_component | nucleus |
| M | 0006355 | biological_process | regulation of DNA-templated transcription |
| M | 0031509 | biological_process | subtelomeric heterochromatin formation |
| M | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
| M | 0048188 | cellular_component | Set1C/COMPASS complex |
| N | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
| O | 0000723 | biological_process | telomere maintenance |
| O | 0000781 | cellular_component | chromosome, telomeric region |
| O | 0000976 | molecular_function | transcription cis-regulatory region binding |
| O | 0005515 | molecular_function | protein binding |
| O | 0005634 | cellular_component | nucleus |
| O | 0031509 | biological_process | subtelomeric heterochromatin formation |
| O | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
| O | 0048188 | cellular_component | Set1C/COMPASS complex |
| P | 0000781 | cellular_component | chromosome, telomeric region |
| P | 0005515 | molecular_function | protein binding |
| P | 0005634 | cellular_component | nucleus |
| P | 0031509 | biological_process | subtelomeric heterochromatin formation |
| P | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
| P | 0048188 | cellular_component | Set1C/COMPASS complex |
| Q | 0000781 | cellular_component | chromosome, telomeric region |
| Q | 0005515 | molecular_function | protein binding |
| Q | 0005634 | cellular_component | nucleus |
| Q | 0031509 | biological_process | subtelomeric heterochromatin formation |
| Q | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
| Q | 0048188 | cellular_component | Set1C/COMPASS complex |
| R | 0000781 | cellular_component | chromosome, telomeric region |
| R | 0003682 | molecular_function | chromatin binding |
| R | 0005515 | molecular_function | protein binding |
| R | 0005634 | cellular_component | nucleus |
| R | 0005829 | cellular_component | cytosol |
| R | 0006355 | biological_process | regulation of DNA-templated transcription |
| R | 0008270 | molecular_function | zinc ion binding |
| R | 0031509 | biological_process | subtelomeric heterochromatin formation |
| R | 0042800 | molecular_function | histone H3K4 methyltransferase activity |
| R | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| R | 0046872 | molecular_function | metal ion binding |
| R | 0048188 | cellular_component | Set1C/COMPASS complex |
| R | 0140002 | molecular_function | histone H3K4me3 reader activity |
| R | 1903341 | biological_process | regulation of meiotic DNA double-strand break formation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN N 1101 |
| Chain | Residue |
| N | CYS1019 |
| N | CYS1068 |
| N | CYS1070 |
| N | CYS1075 |
| N | LYS1076 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue SAM N 1102 |
| Chain | Residue |
| N | SER992 |
| N | TYR993 |
| N | ARG1013 |
| N | ASN1016 |
| N | HIS1017 |
| N | TYR1054 |
| N | LEU1069 |
| N | LEU1079 |
| N | ILE947 |
| N | HIS948 |
| N | TRP950 |
| N | SER991 |
Functional Information from PROSITE/UniProt
| site_id | PS00046 |
| Number of Residues | 7 |
| Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
| Chain | Residue | Details |
| C | ALA21-VAL27 |
| site_id | PS00047 |
| Number of Residues | 5 |
| Details | HISTONE_H4 Histone H4 signature. GAKRH |
| Chain | Residue | Details |
| B | GLY14-HIS18 |
| site_id | PS00299 |
| Number of Residues | 26 |
| Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
| Chain | Residue | Details |
| K | LYS27-ASP52 |
| site_id | PS00322 |
| Number of Residues | 7 |
| Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
| Chain | Residue | Details |
| A | LYS14-LEU20 |
| site_id | PS00357 |
| Number of Residues | 23 |
| Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
| Chain | Residue | Details |
| D | ARG92-GLY114 |
| site_id | PS00678 |
| Number of Residues | 15 |
| Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLTSsrDwSIKLWDL |
| Chain | Residue | Details |
| M | LEU87-LEU101 | |
| L | LEU111-THR125 |
| site_id | PS00959 |
| Number of Residues | 9 |
| Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
| Chain | Residue | Details |
| A | PRO66-ILE74 |
| site_id | PS01359 |
| Number of Residues | 45 |
| Details | ZF_PHD_1 Zinc finger PHD-type signature. Ci.Ckrpdygelm....................................VgCdg..Cddw.FHftClhipeqfkdlvfs................................FyCpyC |
| Chain | Residue | Details |
| R | CYS25-CYS69 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 5 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 79 |
| Details | Repeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 78 |
| Details | Repeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 81 |
| Details | Repeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 84 |
| Details | Repeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI31 |
| Number of Residues | 80 |
| Details | Repeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI32 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31922488","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VEN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI33 |
| Number of Residues | 117 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI34 |
| Number of Residues | 5 |
| Details | Motif: {"description":"RxxxRR motif","evidences":[{"source":"PubMed","id":"31922488","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VEN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI35 |
| Number of Residues | 10 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI36 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI37 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31922488","evidenceCode":"ECO:0000303"},{"source":"PDB","id":"6VEN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI38 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
