Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0007269 | biological_process | neurotransmitter secretion |
| A | 0008021 | cellular_component | synaptic vesicle |
| B | 0005524 | molecular_function | ATP binding |
| B | 0007269 | biological_process | neurotransmitter secretion |
| B | 0008021 | cellular_component | synaptic vesicle |
| C | 0005524 | molecular_function | ATP binding |
| C | 0007269 | biological_process | neurotransmitter secretion |
| C | 0008021 | cellular_component | synaptic vesicle |
| D | 0005524 | molecular_function | ATP binding |
| D | 0007269 | biological_process | neurotransmitter secretion |
| D | 0008021 | cellular_component | synaptic vesicle |
| E | 0005524 | molecular_function | ATP binding |
| E | 0007269 | biological_process | neurotransmitter secretion |
| E | 0008021 | cellular_component | synaptic vesicle |
| F | 0005524 | molecular_function | ATP binding |
| F | 0007269 | biological_process | neurotransmitter secretion |
| F | 0008021 | cellular_component | synaptic vesicle |
| G | 0005524 | molecular_function | ATP binding |
| G | 0007269 | biological_process | neurotransmitter secretion |
| G | 0008021 | cellular_component | synaptic vesicle |
| H | 0005524 | molecular_function | ATP binding |
| H | 0007269 | biological_process | neurotransmitter secretion |
| H | 0008021 | cellular_component | synaptic vesicle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 817 |
| Chain | Residue |
| A | GLU373 |
| A | GLU386 |
| A | ATP800 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 817 |
| Chain | Residue |
| B | GLU373 |
| B | GLU386 |
| B | ATP801 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C 817 |
| Chain | Residue |
| C | GLU373 |
| C | GLU386 |
| C | ATP802 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA D 817 |
| Chain | Residue |
| D | GLU373 |
| D | GLU386 |
| D | ATP803 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA E 817 |
| Chain | Residue |
| E | GLU373 |
| E | GLU386 |
| E | ATP804 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA F 817 |
| Chain | Residue |
| F | GLU373 |
| F | GLU386 |
| F | ATP805 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA G 817 |
| Chain | Residue |
| G | GLU373 |
| G | GLU386 |
| G | ATP806 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA H 817 |
| Chain | Residue |
| H | GLU373 |
| H | GLU386 |
| H | ATP807 |
| H | HOH842 |
| site_id | AC9 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ATP A 800 |
| Chain | Residue |
| A | LYS225 |
| A | VAL267 |
| A | LYS269 |
| A | HIS274 |
| A | SER275 |
| A | GLY276 |
| A | LYS279 |
| A | GLU305 |
| A | PRO306 |
| A | ILE308 |
| A | ASP313 |
| A | ARG328 |
| A | TRP335 |
| A | LYS336 |
| A | THR337 |
| A | ASN338 |
| A | GLU373 |
| A | LEU375 |
| A | GLU386 |
| A | VAL388 |
| A | CA817 |
| A | HOH831 |
| A | HOH859 |
| A | HOH903 |
| A | HOH916 |
| A | HOH935 |
| site_id | BC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ATP B 801 |
| Chain | Residue |
| B | LYS225 |
| B | VAL267 |
| B | LYS269 |
| B | HIS274 |
| B | SER275 |
| B | GLY276 |
| B | LYS279 |
| B | GLU305 |
| B | PRO306 |
| B | PHE307 |
| B | ILE308 |
| B | ASP313 |
| B | ARG328 |
| B | TRP335 |
| B | LYS336 |
| B | THR337 |
| B | ASN338 |
| B | GLU373 |
| B | LEU375 |
| B | ILE385 |
| B | GLU386 |
| B | VAL388 |
| B | CA817 |
| B | HOH842 |
| B | HOH890 |
| B | HOH900 |
| site_id | BC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP C 802 |
| Chain | Residue |
| C | LYS225 |
| C | ILE247 |
| C | VAL267 |
| C | LYS269 |
| C | HIS274 |
| C | SER275 |
| C | GLY276 |
| C | LYS279 |
| C | GLU305 |
| C | PRO306 |
| C | PHE307 |
| C | ILE308 |
| C | ARG328 |
| C | TRP335 |
| C | GLU373 |
| C | LEU375 |
| C | GLU386 |
| C | CA817 |
| site_id | BC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ATP D 803 |
| Chain | Residue |
| D | HIS274 |
| D | SER275 |
| D | GLY276 |
| D | LYS279 |
| D | GLU305 |
| D | PRO306 |
| D | PHE307 |
| D | ILE308 |
| D | ASP313 |
| D | ARG328 |
| D | TRP335 |
| D | LYS336 |
| D | THR337 |
| D | ASN338 |
| D | GLU373 |
| D | LEU375 |
| D | ILE385 |
| D | GLU386 |
| D | CA817 |
| D | HOH869 |
| D | HOH874 |
| D | HOH892 |
| D | LYS225 |
| D | ILE247 |
| D | VAL267 |
| D | LYS269 |
| site_id | BC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP E 804 |
| Chain | Residue |
| E | LYS225 |
| E | ILE247 |
| E | VAL267 |
| E | LYS269 |
| E | HIS274 |
| E | SER275 |
| E | GLY276 |
| E | LYS279 |
| E | GLU305 |
| E | PRO306 |
| E | PHE307 |
| E | ILE308 |
| E | ARG328 |
| E | TRP335 |
| E | LYS336 |
| E | THR337 |
| E | GLU373 |
| E | LEU375 |
| E | GLU386 |
| E | CA817 |
| E | HOH870 |
| site_id | BC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ATP F 805 |
| Chain | Residue |
| F | LYS225 |
| F | ILE247 |
| F | VAL267 |
| F | LYS269 |
| F | ALA273 |
| F | HIS274 |
| F | SER275 |
| F | GLY276 |
| F | LYS279 |
| F | GLU305 |
| F | PRO306 |
| F | PHE307 |
| F | ILE308 |
| F | ASP313 |
| F | ARG328 |
| F | TRP335 |
| F | LYS336 |
| F | THR337 |
| F | GLU373 |
| F | LEU375 |
| F | GLU386 |
| F | VAL388 |
| F | CA817 |
| F | HOH848 |
| site_id | BC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ATP G 806 |
| Chain | Residue |
| G | LYS225 |
| G | ILE247 |
| G | VAL267 |
| G | LYS269 |
| G | HIS274 |
| G | SER275 |
| G | GLY276 |
| G | LYS279 |
| G | GLU305 |
| G | PRO306 |
| G | PHE307 |
| G | ILE308 |
| G | ASP313 |
| G | ARG328 |
| G | TRP335 |
| G | LYS336 |
| G | THR337 |
| G | ASN338 |
| G | GLU373 |
| G | LEU375 |
| G | GLU386 |
| G | CA817 |
| G | HOH880 |
| G | HOH885 |
| site_id | BC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP H 807 |
| Chain | Residue |
| H | LYS225 |
| H | ILE247 |
| H | VAL267 |
| H | LYS269 |
| H | HIS274 |
| H | SER275 |
| H | GLY276 |
| H | LYS279 |
| H | GLU305 |
| H | PRO306 |
| H | PHE307 |
| H | ILE308 |
| H | ARG328 |
| H | TRP335 |
| H | GLU373 |
| H | LEU375 |
| H | GLU386 |
| H | VAL388 |
| H | CA817 |
| H | HOH842 |
| H | HOH855 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 818 |
| Chain | Residue |
| A | HIS217 |
| A | PHE364 |
| A | HOH879 |
| A | HOH902 |
| B | HIS217 |
| B | PHE364 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 819 |
| Chain | Residue |
| B | ASP120 |
| B | THR124 |
| B | TRP126 |
| B | ARG186 |
| B | HOH896 |
Functional Information from PROSITE/UniProt
| site_id | PS00415 |
| Number of Residues | 8 |
| Details | SYNAPSIN_1 Synapsins signature 1. LRRRLSDS |
| Chain | Residue | Details |
| A | LEU4-SER11 | |
| site_id | PS00416 |
| Number of Residues | 11 |
| Details | SYNAPSIN_2 Synapsins signature 2. GHAHSGMGKVK |
| Chain | Residue | Details |
| A | GLY271-LYS281 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O88935","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"12438562","evidenceCode":"ECO:0000269"}]} |