3C1B
The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure
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 | 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 | 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 | 0046982 | molecular_function | protein heterodimerization activity |
D | 0000786 | cellular_component | nucleosome |
D | 0003677 | molecular_function | DNA binding |
D | 0005634 | cellular_component | nucleus |
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 | 0005654 | cellular_component | nucleoplasm |
E | 0005694 | cellular_component | chromosome |
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 | 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 | 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 | 0046982 | molecular_function | protein heterodimerization activity |
H | 0000786 | cellular_component | nucleosome |
H | 0003677 | molecular_function | DNA binding |
H | 0005634 | cellular_component | nucleus |
H | 0005694 | cellular_component | chromosome |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00047 |
Number of Residues | 5 |
Details | HISTONE_H4 Histone H4 signature. GAKRH |
Chain | Residue | Details |
B | GLY14-HIS18 |
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
C | ALA821-VAL827 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG1289-GLY1311 |
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
A | LYS414-LEU420 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO466-ILE474 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250 |
Chain | Residue | Details |
C | SER801 | |
G | SER1001 | |
E | ARG602 | |
E | ARG617 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250 |
Chain | Residue | Details |
C | LYS805 | |
G | LYS1005 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS809 | |
C | LYS895 | |
G | LYS1009 | |
G | LYS1095 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS836 | |
G | LYS1036 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS874 | |
C | LYS875 | |
G | LYS1074 | |
G | LYS1075 | |
F | LYS208 | |
F | LYS216 | |
F | LYS244 | |
F | LYS279 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N5-methylglutamine => ECO:0000250 |
Chain | Residue | Details |
C | GLN904 | |
G | GLN1104 | |
F | LYS212 | |
F | ML3220 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS918 | |
G | LYS1118 | |
F | LYS231 | |
F | LYS291 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 |
Chain | Residue | Details |
C | LYS813 | |
F | SER247 | |
C | LYS815 | |
C | LYS919 | |
G | LYS1013 | |
G | LYS1015 | |
G | LYS1119 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
B | TYR51 | |
E | LYS664 | |
B | TYR88 | |
F | TYR251 | |
F | TYR288 | |
A | LYS464 | |
E | LYS618 | |
E | LYS623 | |
E | LYS627 | |
E | LYS636 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
B | LYS59 | |
F | LYS259 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
B | LYS77 | |
F | LYS277 | |
E | LYS656 | |
E | LYS679 |
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 |
B | LYS31 | |
F | LYS231 |
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 |
A | THR480 | |
B | LYS91 | |
A | THR507 | |
F | LYS291 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS515 | |
E | LYS715 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS522 | |
E | LYS722 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250 |
Chain | Residue | Details |
A | ARG408 | |
E | ARG608 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | ARG426 | |
E | ARG626 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER428 | |
E | SER628 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | LYS437 | |
E | LYS637 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER486 | |
E | SER686 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | CYS510 | |
E | CYS710 |