Functional Information from PROSITE/UniProt
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
N | ALA23-VAL29 |
site_id | PS00141 |
Number of Residues | 12 |
Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LILDSGATHTTA |
Chain | Residue | Details |
L | LEU168-ALA179 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
O | ARG92-GLY114 |
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
J | TYR53-GLY63 |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WISKqEYEE |
Chain | Residue | Details |
L | TRP410-GLU418 | |
J | TRP356-GLU364 |
site_id | PS01132 |
Number of Residues | 13 |
Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
Chain | Residue | Details |
J | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylproline => ECO:0000250|UniProtKB:P23527 |
Chain | Residue | Details |
O | PRO1 | |
N | LYS7 | |
A | GLY70 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosyl glutamic acid => ECO:0000269|PubMed:27530147 |
Chain | Residue | Details |
O | GLU2 | |
N | LYS13 | |
H | LYS673 | |
G | SER321 | |
G | SER755 | |
G | SER928 | |
G | SER1011 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 |
Chain | Residue | Details |
O | LYS5 | |
O | LYS11 | |
O | LYS15 | |
O | LYS16 | |
O | LYS20 | |
O | LYS23 | |
O | LYS43 | |
O | LYS85 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:34874266 |
Chain | Residue | Details |
O | SER6 | |
F | LYS444 | |
F | LYS456 | |
G | SER1728 | |
M | LYS62 | |
E | LYS445 | |
D | LYS9 | |
A | LYS445 | |
D | LYS444 | |
D | LYS456 | |
F | LYS9 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 |
Chain | Residue | Details |
O | LYS12 | |
E | LYS225 | |
A | LYS225 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 |
Chain | Residue | Details |
O | SER14 | |
G | LYS2349 | |
G | LYS2356 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 |
Chain | Residue | Details |
O | LYS24 | |
J | GLU270 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
O | LYS34 | |
O | LYS116 | |
O | LYS120 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 |
Chain | Residue | Details |
O | GLU35 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 |
Chain | Residue | Details |
O | SER36 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62807 |
Chain | Residue | Details |
O | LYS46 | |
O | LYS108 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 |
Chain | Residue | Details |
O | LYS57 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 |
Chain | Residue | Details |
O | ARG79 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 |
Chain | Residue | Details |
O | ARG86 | |
O | ARG92 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729 |
Chain | Residue | Details |
O | THR115 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 |
Chain | Residue | Details |
O | SER112 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P58876 |
Chain | Residue | Details |
O | LYS5 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16713563 |
Chain | Residue | Details |
O | LYS120 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6 |
Chain | Residue | Details |
O | LYS20 |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 |
Chain | Residue | Details |
O | LYS34 |