8ONS
TAF15 amyloid fold in atypical FTLD - Individual 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003712 | molecular_function | transcription coregulator activity |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003730 | molecular_function | mRNA 3'-UTR binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0008380 | biological_process | RNA splicing |
| A | 0010467 | biological_process | gene expression |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048255 | biological_process | mRNA stabilization |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003712 | molecular_function | transcription coregulator activity |
| C | 0003723 | molecular_function | RNA binding |
| C | 0003730 | molecular_function | mRNA 3'-UTR binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005730 | cellular_component | nucleolus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0008380 | biological_process | RNA splicing |
| C | 0010467 | biological_process | gene expression |
| C | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048255 | biological_process | mRNA stabilization |
| E | 0003676 | molecular_function | nucleic acid binding |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003712 | molecular_function | transcription coregulator activity |
| E | 0003723 | molecular_function | RNA binding |
| E | 0003730 | molecular_function | mRNA 3'-UTR binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005654 | cellular_component | nucleoplasm |
| E | 0005730 | cellular_component | nucleolus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0008380 | biological_process | RNA splicing |
| E | 0010467 | biological_process | gene expression |
| E | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0048255 | biological_process | mRNA stabilization |
| G | 0003676 | molecular_function | nucleic acid binding |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003712 | molecular_function | transcription coregulator activity |
| G | 0003723 | molecular_function | RNA binding |
| G | 0003730 | molecular_function | mRNA 3'-UTR binding |
| G | 0005515 | molecular_function | protein binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005654 | cellular_component | nucleoplasm |
| G | 0005730 | cellular_component | nucleolus |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0008380 | biological_process | RNA splicing |
| G | 0010467 | biological_process | gene expression |
| G | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0048255 | biological_process | mRNA stabilization |
| I | 0003676 | molecular_function | nucleic acid binding |
| I | 0003677 | molecular_function | DNA binding |
| I | 0003712 | molecular_function | transcription coregulator activity |
| I | 0003723 | molecular_function | RNA binding |
| I | 0003730 | molecular_function | mRNA 3'-UTR binding |
| I | 0005515 | molecular_function | protein binding |
| I | 0005634 | cellular_component | nucleus |
| I | 0005654 | cellular_component | nucleoplasm |
| I | 0005730 | cellular_component | nucleolus |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006355 | biological_process | regulation of DNA-templated transcription |
| I | 0008380 | biological_process | RNA splicing |
| I | 0010467 | biological_process | gene expression |
| I | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0048255 | biological_process | mRNA stabilization |
Functional Information from PROSITE/UniProt
| site_id | PS01358 |
| Number of Residues | 22 |
| Details | ZF_RANBP2_1 Zinc finger RanBP2-type signature. WvCpnpsCgnmNfarrnsCnqC |
| Chain | Residue | Details |
| A | TRP358-CYS379 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 155 |
| Details | ZN_FING: RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322 |
| Chain | Residue | Details |
| A | LYS354-GLU385 | |
| C | LYS354-GLU385 | |
| E | LYS354-GLU385 | |
| G | LYS354-GLU385 | |
| I | LYS354-GLU385 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | MOD_RES: Omega-N-methylarginine; alternate => ECO:0007744|PubMed:24129315 |
| Chain | Residue | Details |
| A | ARG206 | |
| C | ARG206 | |
| E | ARG206 | |
| G | ARG206 | |
| I | ARG206 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | SER226 | |
| I | SER231 | |
| A | SER231 | |
| C | SER226 | |
| C | SER231 | |
| E | SER226 | |
| E | SER231 | |
| G | SER226 | |
| G | SER231 | |
| I | SER226 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS268 | |
| C | LYS268 | |
| E | LYS268 | |
| G | LYS268 | |
| I | LYS268 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER375 | |
| C | SER375 | |
| E | SER375 | |
| G | SER375 | |
| I | SER375 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER423 | |
| E | SER442 | |
| E | SER451 | |
| E | SER554 | |
| G | SER423 | |
| G | SER442 | |
| G | SER451 | |
| G | SER554 | |
| I | SER423 | |
| I | SER442 | |
| I | SER451 | |
| A | SER442 | |
| I | SER554 | |
| A | SER451 | |
| A | SER554 | |
| C | SER423 | |
| C | SER442 | |
| C | SER451 | |
| C | SER554 | |
| E | SER423 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315 |
| Chain | Residue | Details |
| A | ARG431 | |
| E | ARG459 | |
| E | ARG475 | |
| E | ARG562 | |
| G | ARG431 | |
| G | ARG459 | |
| G | ARG475 | |
| G | ARG562 | |
| I | ARG431 | |
| I | ARG459 | |
| I | ARG475 | |
| A | ARG459 | |
| I | ARG562 | |
| A | ARG475 | |
| A | ARG562 | |
| C | ARG431 | |
| C | ARG459 | |
| C | ARG475 | |
| C | ARG562 | |
| E | ARG431 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER433 | |
| C | SER433 | |
| E | SER433 | |
| G | SER433 | |
| I | SER433 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 5 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER438 | |
| C | SER438 | |
| E | SER438 | |
| G | SER438 | |
| I | SER438 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 5 |
| Details | MOD_RES: Dimethylated arginine => ECO:0000269|Ref.9 |
| Chain | Residue | Details |
| A | ARG483 | |
| C | ARG483 | |
| E | ARG483 | |
| G | ARG483 | |
| I | ARG483 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 10 |
| Details | MOD_RES: Asymmetric dimethylarginine; by PRMT1 => ECO:0000269|PubMed:19124016 |
| Chain | Residue | Details |
| A | ARG528 | |
| I | ARG535 | |
| A | ARG535 | |
| C | ARG528 | |
| C | ARG535 | |
| E | ARG528 | |
| E | ARG535 | |
| G | ARG528 | |
| G | ARG535 | |
| I | ARG528 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 5 |
| Details | MOD_RES: Asymmetric dimethylarginine; by PRMT1 => ECO:0000269|PubMed:19124016, ECO:0000269|Ref.9 |
| Chain | Residue | Details |
| A | ARG570 | |
| C | ARG570 | |
| E | ARG570 | |
| G | ARG570 | |
| I | ARG570 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 5 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS265 | |
| C | LYS265 | |
| E | LYS265 | |
| G | LYS265 | |
| I | LYS265 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 10 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| I | LYS268 | |
| A | LYS268 | |
| C | LYS268 | |
| E | LYS268 | |
| G | LYS268 |
