7X3W
Cryo-EM structure of ISW1-N1 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 | 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 | 0005515 | molecular_function | protein 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 | 0005515 | molecular_function | protein 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 |
K | 0000182 | molecular_function | rDNA binding |
K | 0000976 | molecular_function | transcription cis-regulatory region binding |
K | 0001178 | biological_process | regulation of transcriptional start site selection at RNA polymerase II promoter |
K | 0003677 | molecular_function | DNA binding |
K | 0003730 | molecular_function | mRNA 3'-UTR binding |
K | 0004386 | molecular_function | helicase activity |
K | 0005515 | molecular_function | protein binding |
K | 0005524 | molecular_function | ATP binding |
K | 0005634 | cellular_component | nucleus |
K | 0006325 | biological_process | chromatin organization |
K | 0006338 | biological_process | chromatin remodeling |
K | 0006354 | biological_process | DNA-templated transcription elongation |
K | 0006355 | biological_process | regulation of DNA-templated transcription |
K | 0006363 | biological_process | termination of RNA polymerase I transcription |
K | 0006369 | biological_process | termination of RNA polymerase II transcription |
K | 0007062 | biological_process | sister chromatid cohesion |
K | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
K | 0009408 | biological_process | response to heat |
K | 0016587 | cellular_component | Isw1 complex |
K | 0016787 | molecular_function | hydrolase activity |
K | 0016887 | molecular_function | ATP hydrolysis activity |
K | 0030874 | cellular_component | nucleolar chromatin |
K | 0031491 | molecular_function | nucleosome binding |
K | 0036436 | cellular_component | Isw1a complex |
K | 0036437 | cellular_component | Isw1b complex |
K | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
K | 0046832 | biological_process | negative regulation of RNA export from nucleus |
K | 0140658 | molecular_function | ATP-dependent chromatin remodeler activity |
K | 1902275 | biological_process | regulation of chromatin organization |
K | 1903895 | biological_process | negative regulation of IRE1-mediated unfolded protein response |
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 | 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 | ARG89-GLY111 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | ARG2 | |
A | ARG17 | |
E | ARG2 | |
E | ARG17 | |
H | LYS2 | |
H | LYS9 | |
H | LYS12 | |
H | LYS17 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR3 | |
E | THR3 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181 |
Chain | Residue | Details |
A | LYS4 | |
E | LYS4 | |
G | LYS9 | |
G | LYS95 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | GLN5 | |
E | GLN5 | |
H | LYS117 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR6 | |
A | THR11 | |
E | THR6 | |
E | THR11 | |
F | LYS8 | |
F | LYS16 | |
F | LYS44 | |
F | LYS79 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250 |
Chain | Residue | Details |
A | ARG8 | |
E | ARG8 | |
F | LYS12 | |
F | LYS20 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181 |
Chain | Residue | Details |
A | LYS9 | |
E | LYS9 | |
F | LYS31 | |
F | LYS91 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER10 | |
E | SER10 | |
C | LYS15 | |
C | LYS119 | |
G | LYS13 | |
G | LYS15 | |
G | LYS119 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
A | LYS14 | |
E | LYS14 | |
F | TYR51 | |
F | TYR88 |
site_id | SWS_FT_FI10 |
Number of Residues | 10 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS18 | |
E | LYS64 | |
A | LYS23 | |
A | LYS27 | |
A | LYS36 | |
A | LYS64 | |
E | LYS18 | |
E | LYS23 | |
E | LYS27 | |
E | LYS36 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | ARG26 | |
E | ARG26 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER28 | |
E | SER28 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | LYS37 | |
E | LYS37 | |
F | LYS91 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | TYR41 | |
E | TYR41 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
A | LYS56 | |
A | LYS79 | |
E | LYS56 | |
E | LYS79 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER57 | |
E | SER57 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR80 | |
A | THR107 | |
E | THR80 | |
E | THR107 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER86 | |
E | SER86 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS115 | |
E | LYS115 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS122 | |
E | LYS122 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | CYS110 | |
E | CYS110 |