7AT8
Histone H3 recognition by nucleosome-bound PRC2 subunit EZH2.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006338 | biological_process | chromatin remodeling |
A | 0042054 | molecular_function | histone methyltransferase activity |
A | 0046976 | molecular_function | histone H3K27 methyltransferase activity |
C | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
C | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
C | 0001222 | molecular_function | transcription corepressor binding |
C | 0001739 | cellular_component | sex chromatin |
C | 0003682 | molecular_function | chromatin binding |
C | 0003723 | molecular_function | RNA binding |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005677 | cellular_component | chromatin silencing complex |
C | 0005730 | cellular_component | nucleolus |
C | 0006325 | biological_process | chromatin organization |
C | 0008047 | molecular_function | enzyme activator activity |
C | 0008283 | biological_process | cell population proliferation |
C | 0008284 | biological_process | positive regulation of cell population proliferation |
C | 0016586 | cellular_component | RSC-type complex |
C | 0016604 | cellular_component | nuclear body |
C | 0031490 | molecular_function | chromatin DNA binding |
C | 0032993 | cellular_component | protein-DNA complex |
C | 0035064 | molecular_function | methylated histone binding |
C | 0035098 | cellular_component | ESC/E(Z) complex |
C | 0043565 | molecular_function | sequence-specific DNA binding |
C | 0045596 | biological_process | negative regulation of cell differentiation |
C | 0046872 | molecular_function | metal ion binding |
C | 0048709 | biological_process | oligodendrocyte differentiation |
C | 0060816 | biological_process | random inactivation of X chromosome |
C | 0106222 | molecular_function | lncRNA binding |
C | 0140718 | biological_process | facultative heterochromatin formation |
C | 1990841 | molecular_function | promoter-specific chromatin binding |
C | 1990904 | cellular_component | ribonucleoprotein complex |
D | 0000786 | cellular_component | nucleosome |
D | 0003677 | molecular_function | DNA binding |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005694 | cellular_component | chromosome |
D | 0030527 | molecular_function | structural constituent of chromatin |
D | 0046982 | molecular_function | protein heterodimerization activity |
E | 0000786 | cellular_component | nucleosome |
E | 0003677 | molecular_function | DNA binding |
E | 0005515 | molecular_function | protein binding |
E | 0005634 | cellular_component | nucleus |
E | 0005694 | cellular_component | chromosome |
E | 0006334 | biological_process | nucleosome assembly |
E | 0030527 | molecular_function | structural constituent of chromatin |
E | 0046982 | molecular_function | protein heterodimerization activity |
F | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0005634 | cellular_component | nucleus |
F | 0005694 | cellular_component | chromosome |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0046982 | molecular_function | protein heterodimerization activity |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0005515 | molecular_function | protein binding |
G | 0005634 | cellular_component | nucleus |
G | 0005694 | cellular_component | chromosome |
G | 0030527 | molecular_function | structural constituent of chromatin |
G | 0046982 | molecular_function | protein heterodimerization activity |
H | 0000786 | cellular_component | nucleosome |
H | 0003677 | molecular_function | DNA binding |
H | 0005515 | molecular_function | protein binding |
H | 0005634 | cellular_component | nucleus |
H | 0005654 | cellular_component | nucleoplasm |
H | 0005694 | cellular_component | chromosome |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
I | 0000786 | cellular_component | nucleosome |
I | 0003677 | molecular_function | DNA binding |
I | 0005515 | molecular_function | protein binding |
I | 0005634 | cellular_component | nucleus |
I | 0005694 | cellular_component | chromosome |
I | 0006334 | biological_process | nucleosome assembly |
I | 0030527 | molecular_function | structural constituent of chromatin |
I | 0046982 | molecular_function | protein heterodimerization activity |
J | 0000786 | cellular_component | nucleosome |
J | 0003677 | molecular_function | DNA binding |
J | 0005634 | cellular_component | nucleus |
J | 0005694 | cellular_component | chromosome |
J | 0030527 | molecular_function | structural constituent of chromatin |
J | 0046982 | molecular_function | protein heterodimerization activity |
K | 0000786 | cellular_component | nucleosome |
K | 0003677 | molecular_function | DNA binding |
K | 0005515 | molecular_function | protein binding |
K | 0005634 | cellular_component | nucleus |
K | 0005694 | cellular_component | chromosome |
K | 0030527 | molecular_function | structural constituent of chromatin |
K | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00028 |
Number of Residues | 22 |
Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cpw..CtlnCrklysllkHlklc.H |
Chain | Residue | Details |
C | CYS450-HIS471 |
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
F | ALA21-VAL27 |
site_id | PS00047 |
Number of Residues | 5 |
Details | HISTONE_H4 Histone H4 signature. GAKRH |
Chain | Residue | Details |
E | GLY14-HIS18 |
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
D | LYS14-LEU20 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
G | ARG89-GLY111 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
D | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKB/AKT1 => ECO:0000269|PubMed:16224021 |
Chain | Residue | Details |
A | SER21 | |
J | SER1 | |
G | LYS12 | |
G | LYS17 | |
K | LYS2 | |
K | LYS9 | |
K | LYS12 | |
K | LYS17 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER76 | |
A | SER368 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR344 | |
F | LYS95 | |
J | LYS9 | |
J | LYS95 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CDK1 and CDK2 => ECO:0000269|PubMed:20935635 |
Chain | Residue | Details |
A | THR350 | |
J | LYS36 | |
K | LYS117 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER371 | |
F | LYS75 | |
J | LYS74 | |
J | LYS75 | |
I | LYS8 | |
I | LYS16 | |
I | LYS44 | |
I | LYS79 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR372 | |
J | GLN104 | |
I | LYS12 | |
I | LYS20 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR505 | |
J | LYS118 | |
I | LYS31 | |
I | LYS91 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:24474760 |
Chain | Residue | Details |
A | SER75 | |
I | SER47 | |
F | LYS15 | |
F | LYS119 | |
J | LYS13 | |
J | LYS15 | |
J | LYS119 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS652 | |
E | TYR88 | |
I | TYR51 | |
I | TYR88 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
E | LYS59 | |
H | LYS64 | |
I | LYS59 | |
D | LYS27 | |
D | LYS36 | |
D | LYS64 | |
H | LYS18 | |
H | LYS23 | |
H | LYS27 | |
H | LYS36 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
E | LYS77 | |
I | LYS77 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
E | LYS31 | |
I | LYS31 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | LYS37 | |
E | LYS91 | |
I | LYS91 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
D | TYR41 | |
H | TYR41 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
D | LYS56 | |
D | LYS79 | |
H | LYS56 | |
H | LYS79 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
D | SER57 | |
H | SER57 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
D | THR80 | |
D | THR107 | |
H | THR80 | |
H | THR107 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
D | SER86 | |
H | SER86 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
D | LYS115 | |
H | LYS115 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
D | LYS122 | |
H | LYS122 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
D | CYS110 | |
H | CYS110 |