8E3I
CRYO-EM STRUCTURE OF the human MPSF IN COMPLEX WITH THE AUUAAA poly(A) signal
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003723 | molecular_function | RNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005847 | cellular_component | mRNA cleavage and polyadenylation specificity factor complex |
A | 0006397 | biological_process | mRNA processing |
A | 0019899 | molecular_function | enzyme binding |
A | 0035925 | molecular_function | mRNA 3'-UTR AU-rich region binding |
A | 0180012 | biological_process | co-transcriptional RNA 3'-end processing, cleavage and polyadenylation pathway |
B | 0031124 | biological_process | mRNA 3'-end processing |
C | 0003676 | molecular_function | nucleic acid binding |
C | 0003723 | molecular_function | RNA binding |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005847 | cellular_component | mRNA cleavage and polyadenylation specificity factor complex |
C | 0006397 | biological_process | mRNA processing |
C | 0008270 | molecular_function | zinc ion binding |
C | 0043231 | cellular_component | intracellular membrane-bounded organelle |
C | 0046872 | molecular_function | metal ion binding |
C | 1990837 | molecular_function | sequence-specific double-stranded DNA binding |
Functional Information from PROSITE/UniProt
site_id | PS00213 |
Number of Residues | 13 |
Details | LIPOCALIN Lipocalin signature. EVKl.NLNGNWLLT |
Chain | Residue | Details |
B | GLU293-THR305 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
B | ALA2 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER7 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
B | LYS46 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS526 | |
B | LYS560 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS530 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | MET200 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
C | SER202 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | PRO212 |