2TMA
TROPOMYOSIN CRYSTAL STRUCTURE AND MUSCLE REGULATION. APPENDIX. CONSTRUCTION OF AN ATOMIC MODEL FOR TROPOMYOSIN AND IMPLICATIONS FOR INTERACTIONS WITH ACTIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003779 | molecular_function | actin binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005884 | cellular_component | actin filament |
| A | 0006936 | biological_process | muscle contraction |
| A | 0007015 | biological_process | actin filament organization |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0031013 | molecular_function | troponin I binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0051015 | molecular_function | actin filament binding |
| B | 0003779 | molecular_function | actin binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005884 | cellular_component | actin filament |
| B | 0006936 | biological_process | muscle contraction |
| B | 0007015 | biological_process | actin filament organization |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0031013 | molecular_function | troponin I binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0051015 | molecular_function | actin filament binding |
Functional Information from PROSITE/UniProt
| site_id | PS00326 |
| Number of Residues | 9 |
| Details | TROPOMYOSIN Tropomyosins signature. LKEAEtRAE |
| Chain | Residue | Details |
| A | LEU232-GLU240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:624724, ECO:0000269|PubMed:6993480, ECO:0000269|PubMed:7622625 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04692 |
| Chain | Residue | Details |
| A | SER45 | |
| B | SER45 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09493 |
| Chain | Residue | Details |
| A | SER174 | |
| B | SER174 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P58771 |
| Chain | Residue | Details |
| A | SER186 | |
| A | SER206 | |
| A | SER252 | |
| A | SER271 | |
| B | SER186 | |
| B | SER206 | |
| B | SER252 | |
| B | SER271 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P04692 |
| Chain | Residue | Details |
| A | TYR261 | |
| B | TYR261 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by DAPK1 => ECO:0000269|PubMed:278975 |
| Chain | Residue | Details |
| A | SER283 | |
| B | SER283 |
