8OL1
cGAS-Nucleosome in complex with SPSB3-ELOBC (composite structure)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000786 | cellular_component | nucleosome |
A | 0003677 | molecular_function | DNA binding |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0046982 | molecular_function | protein heterodimerization activity |
B | 0003677 | molecular_function | DNA binding |
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 | 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 | 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 | 0030527 | molecular_function | structural constituent of chromatin |
E | 0046982 | molecular_function | protein heterodimerization activity |
F | 0003677 | molecular_function | DNA binding |
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 | 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 | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
M | 0001222 | molecular_function | transcription corepressor binding |
M | 0005515 | molecular_function | protein binding |
M | 0005634 | cellular_component | nucleus |
M | 0005654 | cellular_component | nucleoplasm |
M | 0005829 | cellular_component | cytosol |
M | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
M | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
M | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
M | 0016567 | biological_process | protein ubiquitination |
M | 0030674 | molecular_function | protein-macromolecule adaptor activity |
M | 0031462 | cellular_component | Cul2-RING ubiquitin ligase complex |
M | 0031466 | cellular_component | Cul5-RING ubiquitin ligase complex |
M | 0070449 | cellular_component | elongin complex |
M | 0140958 | biological_process | target-directed miRNA degradation |
N | 0001222 | molecular_function | transcription corepressor binding |
N | 0005515 | molecular_function | protein binding |
N | 0005634 | cellular_component | nucleus |
N | 0005654 | cellular_component | nucleoplasm |
N | 0005829 | cellular_component | cytosol |
N | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
N | 0006368 | biological_process | transcription elongation by RNA polymerase II |
N | 0016567 | biological_process | protein ubiquitination |
N | 0030891 | cellular_component | VCB complex |
N | 0031462 | cellular_component | Cul2-RING ubiquitin ligase complex |
N | 0031466 | cellular_component | Cul5-RING ubiquitin ligase complex |
N | 0031625 | molecular_function | ubiquitin protein ligase binding |
N | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
N | 0065003 | biological_process | protein-containing complex assembly |
N | 0070449 | cellular_component | elongin complex |
N | 0140958 | biological_process | target-directed miRNA degradation |
Functional Information from PROSITE/UniProt
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
G | ALA21-VAL27 | |
C | ALA21-VAL27 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG92-GLY114 | |
H | ARG92-GLY114 |
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 | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
N | MET1 | |
H | LYS116 | |
H | LYS120 | |
F | LYS31 | |
F | LYS77 | |
F | LYS91 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62869 |
Chain | Residue | Details |
N | THR84 | |
K | SER380 | |
K | LYS414 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62869 |
Chain | Residue | Details |
N | SER108 | |
N | SER111 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0007744|PDB:6CT9, ECO:0007744|PDB:6CTA |
Chain | Residue | Details |
K | ASP319 | |
H | LYS85 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24462292, ECO:0000269|PubMed:31113940, ECO:0007744|PDB:4O67, ECO:0007744|PDB:6MJX |
Chain | Residue | Details |
K | LYS362 | |
K | ARG376 |
Chain | Residue | Details |
K | HIS390 | |
F | LYS79 |
Chain | Residue | Details |
K | CYS396 | |
K | CYS397 | |
K | CYS404 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30007416, ECO:0000305|PubMed:24462292, ECO:0007744|PDB:6CTA |
Chain | Residue | Details |
K | SER435 | |
H | ARG92 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | SITE: Important for preferential detection of curved long DNA => ECO:0000269|PubMed:30007416 |
Chain | Residue | Details |
K | LYS187 | |
K | LEU195 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | SITE: Arginine-anchor => ECO:0000269|PubMed:32911482, ECO:0000269|PubMed:32912999, ECO:0000269|PubMed:33051594 |
Chain | Residue | Details |
K | ARG255 | |
B | LYS91 | |
F | LYS91 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | SITE: Cleavage; by CASP3 => ECO:0000269|PubMed:30878284 |
Chain | Residue | Details |
K | ASP319 | |
B | LYS79 | |
F | LYS59 | |
F | LYS79 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269|PubMed:35460603 |
Chain | Residue | Details |
K | ASP191 | |
H | LYS120 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:30092200 |
Chain | Residue | Details |
K | ASN210 | |
K | ASN389 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:33273464 |
Chain | Residue | Details |
K | SER213 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by BLK => ECO:0000269|PubMed:30356214 |
Chain | Residue | Details |
K | TYR215 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q8C6L5 |
Chain | Residue | Details |
K | GLU286 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CDK1 and PKB => ECO:0000269|PubMed:26440888, ECO:0000269|PubMed:32351706, ECO:0000269|PubMed:33542149 |
Chain | Residue | Details |
K | SER305 |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl glutamate => ECO:0000250|UniProtKB:Q8C6L5 |
Chain | Residue | Details |
K | GLU314 |
site_id | SWS_FT_FI19 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039 |
Chain | Residue | Details |
K | LYS384 | |
K | LYS392 | |
K | LYS394 |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30799039, ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
K | LYS414 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:32474700 |
Chain | Residue | Details |
K | SER434 | |
K | SER435 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: (Microbial infection) Deamidated glutamine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:30092200 |
Chain | Residue | Details |
K | GLN451 | |
K | GLN454 |
site_id | SWS_FT_FI23 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:35210392 |
Chain | Residue | Details |
K | LYS506 |
site_id | SWS_FT_FI24 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:37802025 |
Chain | Residue | Details |
K | CYS404 | |
K | CYS405 |
site_id | SWS_FT_FI25 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:35438208 |
Chain | Residue | Details |
K | CYS474 |
site_id | SWS_FT_FI26 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:28273161 |
Chain | Residue | Details |
K | LYS173 |
site_id | SWS_FT_FI27 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:27637147 |
Chain | Residue | Details |
K | LYS479 |
site_id | SWS_FT_FI28 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:27637147 |
Chain | Residue | Details |
K | LYS231 |
site_id | SWS_FT_FI29 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27637147 |
Chain | Residue | Details |
K | ALA285 |
site_id | SWS_FT_FI30 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:Q8C6L5 |
Chain | Residue | Details |
K | LYS347 |
site_id | SWS_FT_FI31 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:28273161 |
Chain | Residue | Details |
K | LYS384 |
site_id | SWS_FT_FI32 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250|UniProtKB:Q8C6L5 |
Chain | Residue | Details |
K | LYS394 |
site_id | SWS_FT_FI33 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:35503863 |
Chain | Residue | Details |
K | LYS411 |
site_id | SWS_FT_FI34 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27666593 |
Chain | Residue | Details |
K | LYS414 |
site_id | SWS_FT_FI35 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:38418882 |
Chain | Residue | Details |
K | LYS427 | |
K | ALA428 |