Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000785 | cellular_component | chromatin |
| A | 0000786 | cellular_component | nucleosome |
| A | 0000791 | cellular_component | euchromatin |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003680 | molecular_function | minor groove of adenine-thymine-rich DNA binding |
| A | 0003690 | molecular_function | double-stranded DNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005694 | cellular_component | chromosome |
| A | 0005730 | cellular_component | nucleolus |
| A | 0006334 | biological_process | nucleosome assembly |
| A | 0016604 | cellular_component | nuclear body |
| A | 0017053 | cellular_component | transcription repressor complex |
| A | 0030261 | biological_process | chromosome condensation |
| A | 0030527 | molecular_function | structural constituent of chromatin |
| A | 0031490 | molecular_function | chromatin DNA binding |
| A | 0031491 | molecular_function | nucleosome binding |
| A | 0031492 | molecular_function | nucleosomal DNA binding |
| A | 0031507 | biological_process | heterochromatin formation |
| A | 0045910 | biological_process | negative regulation of DNA recombination |
| A | 2000679 | biological_process | positive regulation of transcription regulatory region DNA binding |
| E | 0006338 | biological_process | chromatin remodeling |
| E | 0042054 | molecular_function | histone methyltransferase activity |
| E | 0046976 | molecular_function | histone H3K27 methyltransferase activity |
| G | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| G | 0001222 | molecular_function | transcription corepressor binding |
| G | 0001739 | cellular_component | sex chromatin |
| G | 0003682 | molecular_function | chromatin binding |
| G | 0005515 | molecular_function | protein binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005654 | cellular_component | nucleoplasm |
| G | 0005677 | cellular_component | chromatin silencing complex |
| G | 0005694 | cellular_component | chromosome |
| G | 0006325 | biological_process | chromatin organization |
| G | 0006351 | biological_process | DNA-templated transcription |
| G | 0008047 | molecular_function | enzyme activator activity |
| G | 0021510 | biological_process | spinal cord development |
| G | 0031491 | molecular_function | nucleosome binding |
| G | 0031507 | biological_process | heterochromatin formation |
| G | 0035098 | cellular_component | ESC/E(Z) complex |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0045120 | cellular_component | pronucleus |
| G | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| G | 0140718 | biological_process | facultative heterochromatin formation |
| G | 1990841 | molecular_function | promoter-specific chromatin binding |
| I | 0000786 | cellular_component | nucleosome |
| I | 0003677 | molecular_function | DNA binding |
| I | 0005515 | molecular_function | protein binding |
| I | 0005634 | cellular_component | nucleus |
| I | 0005654 | cellular_component | nucleoplasm |
| I | 0005694 | cellular_component | chromosome |
| I | 0030527 | molecular_function | structural constituent of chromatin |
| I | 0031492 | molecular_function | nucleosomal DNA binding |
| I | 0031507 | biological_process | heterochromatin formation |
| I | 0046982 | molecular_function | protein heterodimerization activity |
| J | 0000786 | cellular_component | nucleosome |
| J | 0003677 | molecular_function | DNA binding |
| J | 0005515 | molecular_function | protein binding |
| J | 0005634 | cellular_component | nucleus |
| J | 0005694 | cellular_component | chromosome |
| J | 0006334 | biological_process | nucleosome assembly |
| J | 0030527 | molecular_function | structural constituent of chromatin |
| J | 0031507 | biological_process | heterochromatin formation |
| J | 0046982 | molecular_function | protein heterodimerization activity |
| O | 0000118 | cellular_component | histone deacetylase complex |
| O | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| O | 0000781 | cellular_component | chromosome, telomeric region |
| O | 0000785 | cellular_component | chromatin |
| O | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| O | 0005515 | molecular_function | protein binding |
| O | 0005634 | cellular_component | nucleus |
| O | 0005654 | cellular_component | nucleoplasm |
| O | 0006260 | biological_process | DNA replication |
| O | 0006281 | biological_process | DNA repair |
| O | 0006325 | biological_process | chromatin organization |
| O | 0006334 | biological_process | nucleosome assembly |
| O | 0006335 | biological_process | DNA replication-dependent chromatin assembly |
| O | 0006338 | biological_process | chromatin remodeling |
| O | 0006351 | biological_process | DNA-templated transcription |
| O | 0006355 | biological_process | regulation of DNA-templated transcription |
| O | 0006974 | biological_process | DNA damage response |
| O | 0007420 | biological_process | brain development |
| O | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
| O | 0008285 | biological_process | negative regulation of cell population proliferation |
| O | 0016581 | cellular_component | NuRD complex |
| O | 0016589 | cellular_component | NURF complex |
| O | 0030336 | biological_process | negative regulation of cell migration |
| O | 0030512 | biological_process | negative regulation of transforming growth factor beta receptor signaling pathway |
| O | 0031492 | molecular_function | nucleosomal DNA binding |
| O | 0031507 | biological_process | heterochromatin formation |
| O | 0032991 | cellular_component | protein-containing complex |
| O | 0033186 | cellular_component | CAF-1 complex |
| O | 0035098 | cellular_component | ESC/E(Z) complex |
| O | 0042393 | molecular_function | histone binding |
| O | 0042659 | biological_process | regulation of cell fate specification |
| O | 0042826 | molecular_function | histone deacetylase binding |
| O | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| O | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| O | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| O | 0070822 | cellular_component | Sin3-type complex |
| O | 1902455 | biological_process | negative regulation of stem cell population maintenance |
| O | 1902459 | biological_process | positive regulation of stem cell population maintenance |
| O | 2000736 | biological_process | regulation of stem cell differentiation |
| R | 0000786 | cellular_component | nucleosome |
| R | 0003677 | molecular_function | DNA binding |
| R | 0005634 | cellular_component | nucleus |
| R | 0005694 | cellular_component | chromosome |
| R | 0030527 | molecular_function | structural constituent of chromatin |
| R | 0031507 | biological_process | heterochromatin formation |
| R | 0046982 | molecular_function | protein heterodimerization activity |
| S | 0000786 | cellular_component | nucleosome |
| S | 0002227 | biological_process | innate immune response in mucosa |
| S | 0003677 | molecular_function | DNA binding |
| S | 0005515 | molecular_function | protein binding |
| S | 0005615 | cellular_component | extracellular space |
| S | 0005634 | cellular_component | nucleus |
| S | 0005694 | cellular_component | chromosome |
| S | 0006325 | biological_process | chromatin organization |
| S | 0019731 | biological_process | antibacterial humoral response |
| S | 0030527 | molecular_function | structural constituent of chromatin |
| S | 0031507 | biological_process | heterochromatin formation |
| S | 0046982 | molecular_function | protein heterodimerization activity |
| S | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
| U | 0000786 | cellular_component | nucleosome |
| U | 0003677 | molecular_function | DNA binding |
| U | 0005634 | cellular_component | nucleus |
| U | 0005694 | cellular_component | chromosome |
| U | 0030527 | molecular_function | structural constituent of chromatin |
| U | 0031507 | biological_process | heterochromatin formation |
| U | 0046982 | molecular_function | protein heterodimerization activity |
| V | 0000786 | cellular_component | nucleosome |
| V | 0002227 | biological_process | innate immune response in mucosa |
| V | 0003677 | molecular_function | DNA binding |
| V | 0005515 | molecular_function | protein binding |
| V | 0005615 | cellular_component | extracellular space |
| V | 0005634 | cellular_component | nucleus |
| V | 0005694 | cellular_component | chromosome |
| V | 0006325 | biological_process | chromatin organization |
| V | 0019731 | biological_process | antibacterial humoral response |
| V | 0030527 | molecular_function | structural constituent of chromatin |
| V | 0031507 | biological_process | heterochromatin formation |
| V | 0046982 | molecular_function | protein heterodimerization activity |
| V | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
| W | 0000786 | cellular_component | nucleosome |
| W | 0003677 | molecular_function | DNA binding |
| W | 0005515 | molecular_function | protein binding |
| W | 0005634 | cellular_component | nucleus |
| W | 0005654 | cellular_component | nucleoplasm |
| W | 0005694 | cellular_component | chromosome |
| W | 0030527 | molecular_function | structural constituent of chromatin |
| W | 0031492 | molecular_function | nucleosomal DNA binding |
| W | 0031507 | biological_process | heterochromatin formation |
| W | 0046982 | molecular_function | protein heterodimerization activity |
| X | 0000786 | cellular_component | nucleosome |
| X | 0003677 | molecular_function | DNA binding |
| X | 0005515 | molecular_function | protein binding |
| X | 0005634 | cellular_component | nucleus |
| X | 0005694 | cellular_component | chromosome |
| X | 0006334 | biological_process | nucleosome assembly |
| X | 0030527 | molecular_function | structural constituent of chromatin |
| X | 0031507 | biological_process | heterochromatin formation |
| X | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
| site_id | PS00028 |
| Number of Residues | 24 |
| Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. CcwdqCqacFnsspdladHirsi.H |
| Chain | Residue | Details |
| Y | CYS55-HIS78 | |
| Y | CYS122-HIS144 | |
| D | CYS450-HIS471 |
| site_id | PS00046 |
| Number of Residues | 7 |
| Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
| Chain | Residue | Details |
| R | ALA21-VAL27 |
| site_id | PS00047 |
| Number of Residues | 5 |
| Details | HISTONE_H4 Histone H4 signature. GAKRH |
| Chain | Residue | Details |
| J | GLY14-HIS18 |
| site_id | PS00322 |
| Number of Residues | 7 |
| Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
| Chain | Residue | Details |
| I | LYS14-LEU20 |
| site_id | PS00357 |
| Number of Residues | 23 |
| Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
| Chain | Residue | Details |
| S | ARG89-GLY111 |
| site_id | PS00678 |
| Number of Residues | 15 |
| Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSVskDhALRLWNI |
| Chain | Residue | Details |
| G | LEU206-ILE220 | |
| O | LEU193-ILE207 | |
| O | LEU289-LEU303 | |
| O | LEU333-LEU347 |
| site_id | PS00959 |
| Number of Residues | 9 |
| Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
| Chain | Residue | Details |
| I | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 73 |
| Details | Domain: {"description":"H15","evidences":[{"source":"PROSITE-ProRule","id":"PRU00837","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"P43275","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 23 |
| Details | Zinc finger: {"description":"C2H2-type"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 76 |
| Details | Region: {"description":"VEFS-box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Breakpoint for translocation to form JAZF1-SUZ12 oncogene"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 102 |
| Details | Domain: {"description":"CXC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00970","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 115 |
| Details | Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 29 |
| Details | Region: {"description":"Interaction with EED","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"16224021","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"24474760","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 43 |
| Details | Repeat: {"description":"WD 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 43 |
| Details | Repeat: {"description":"WD 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 40 |
| Details | Repeat: {"description":"WD 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 41 |
| Details | Repeat: {"description":"WD 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"WD 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 40 |
| Details | Repeat: {"description":"WD 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"WD 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 360 |
| Details | Region: {"description":"Interaction with EZH2","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 294 |
| Details | Region: {"description":"Required for interaction with the matrix protein MA of HIV-1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"20974918","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| 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_FI31 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI32 |
| 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_FI33 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI34 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI35 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI36 |
| 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_FI37 |
| 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_FI38 |
| 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_FI39 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI40 |
| 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_FI41 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI42 |
| 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_FI43 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI44 |
| 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_FI45 |
| 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_FI46 |
| 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_FI47 |
| 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_FI48 |
| Number of Residues | 4 |
| Details | DNA binding: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI49 |
| Number of Residues | 49 |
| Details | Repeat: {"description":"WD 2","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI50 |
| Number of Residues | 47 |
| Details | Repeat: {"description":"WD 3","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI51 |
| Number of Residues | 45 |
| Details | Repeat: {"description":"WD 4","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI52 |
| Number of Residues | 43 |
| Details | Repeat: {"description":"WD 5","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI53 |
| Number of Residues | 56 |
| Details | Repeat: {"description":"WD 6","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI54 |
| Number of Residues | 32 |
| Details | Repeat: {"description":"WD 7","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI55 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI56 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI57 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60972","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI58 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI59 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI60 |
| 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_FI61 |
| 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_FI62 |
| 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_FI63 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI64 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI65 |
| Number of Residues | 8 |
| 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_FI66 |
| 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_FI67 |
| 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_FI68 |
| Number of Residues | 71 |
| Details | Region: {"description":"Interaction with SUZ12","evidences":[{"source":"PubMed","id":"29499137","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI69 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
