6CVJ
Model of synthetic tau (four tandem repeats of first repeat sequence) bound to the microtubule
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000226 | biological_process | microtubule cytoskeleton organization |
| A | 0000278 | biological_process | mitotic cell cycle |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005200 | molecular_function | structural constituent of cytoskeleton |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005874 | cellular_component | microtubule |
| A | 0007017 | biological_process | microtubule-based process |
| A | 0015630 | cellular_component | microtubule cytoskeleton |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000226 | biological_process | microtubule cytoskeleton organization |
| B | 0000278 | biological_process | mitotic cell cycle |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005200 | molecular_function | structural constituent of cytoskeleton |
| B | 0005515 | molecular_function | protein binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005874 | cellular_component | microtubule |
| B | 0007017 | biological_process | microtubule-based process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000226 | biological_process | microtubule cytoskeleton organization |
| C | 0000278 | biological_process | mitotic cell cycle |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005200 | molecular_function | structural constituent of cytoskeleton |
| C | 0005515 | molecular_function | protein binding |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005874 | cellular_component | microtubule |
| C | 0007017 | biological_process | microtubule-based process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008017 | molecular_function | microtubule binding |
| D | 0015631 | molecular_function | tubulin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue GTP A 501 |
| Chain | Residue |
| A | GLY10 |
| A | GLY143 |
| A | GLY144 |
| A | THR145 |
| A | GLY146 |
| A | ILE171 |
| A | THR179 |
| A | GLU183 |
| A | ASN206 |
| A | TYR224 |
| A | ASN228 |
| A | GLN11 |
| A | ILE231 |
| A | MG502 |
| B | LYS254 |
| A | ALA12 |
| A | GLN15 |
| A | ASP98 |
| A | ALA99 |
| A | ALA100 |
| A | ASN101 |
| A | SER140 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | GLU71 |
| A | ASP98 |
| A | GTP501 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue GDP B 501 |
| Chain | Residue |
| B | GLN11 |
| B | CYS12 |
| B | GLN15 |
| B | ASN101 |
| B | SER140 |
| B | GLY143 |
| B | GLY144 |
| B | THR145 |
| B | GLY146 |
| B | ASP179 |
| B | ASN206 |
| B | TYR224 |
| B | ASN228 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue GDP C 501 |
| Chain | Residue |
| C | GLN11 |
| C | CYS12 |
| C | GLN15 |
| C | SER140 |
| C | GLY143 |
| C | GLY144 |
| C | THR145 |
| C | GLY146 |
| C | ASP179 |
| C | GLU183 |
| C | ASN206 |
| C | TYR224 |
| C | ASN228 |
Functional Information from PROSITE/UniProt
| site_id | PS00227 |
| Number of Residues | 7 |
| Details | TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG |
| Chain | Residue | Details |
| A | GLY142-GLY148 | |
| B | GLY142-GLY148 |
| site_id | PS00228 |
| Number of Residues | 4 |
| Details | TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI |
| Chain | Residue | Details |
| B | MET1-ILE4 |
| site_id | PS00229 |
| Number of Residues | 13 |
| Details | TAU_MAP_1 Tau and MAP proteins tubulin-binding repeat signature. GSteNlkHqPGGG |
| Chain | Residue | Details |
| D | GLY261-GLY273 | |
| D | GLY293-GLY305 | |
| D | GLY325-GLY337 | |
| D | GLY357-GLY369 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | SITE: Not glycated => ECO:0000269|PubMed:9326300 |
| Chain | Residue | Details |
| D | LYS224 | |
| D | VAL312 | |
| D | ASN319 | |
| D | LYS323 | |
| D | GLN333 | |
| D | ALA342 | |
| D | PRO345 | |
| D | ILE373 | |
| D | LEU378 | |
| D | ALA386 | |
| D | THR388 | |
| D | LYS240 | |
| D | SER398 | |
| D | LYS254 | |
| D | LYS257 | |
| D | LYS267 | |
| D | ARG274 | |
| D | LYS291 | |
| D | THR295 | |
| D | LYS299 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by TTBK1 => ECO:0000269|PubMed:16923168 |
| Chain | Residue | Details |
| D | TYR197 | |
| C | GLU71 | |
| A | SER140 | |
| A | GLY144 | |
| A | THR145 | |
| A | THR179 | |
| A | ASN206 | |
| A | ASN228 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PDPK1 and TTBK1 => ECO:0000269|PubMed:16923168 |
| Chain | Residue | Details |
| D | SER198 | |
| C | SER40 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PDPK1 and TTBK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189 |
| Chain | Residue | Details |
| D | SER199 | |
| C | LYS60 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by CK1, PDPK1 and TTBK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| D | SER202 | |
| C | SER174 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CK1 and PDPK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:19451179 |
| Chain | Residue | Details |
| D | THR205 | |
| B | THR292 | |
| C | THR287 | |
| C | THR292 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:9614189 |
| Chain | Residue | Details |
| D | THR212 | |
| C | ARG320 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189 |
| Chain | Residue | Details |
| D | SER214 | |
| C | GLU448 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179 |
| Chain | Residue | Details |
| D | THR217 | |
| C | LYS60 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10637 |
| Chain | Residue | Details |
| D | LYS225 | |
| D | LYS291 | |
| C | LYS326 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by GSK3-beta and PDPK1 => ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| D | THR231 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| D | SER235 | |
| A | LYS370 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:8999860 |
| Chain | Residue | Details |
| D | SER237 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P10637 |
| Chain | Residue | Details |
| D | LYS259 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by MARK1, MARK2, MARK3, MARK4, BRSK1, BRSK2 and PHK => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:7706316, ECO:0000269|PubMed:8999860, ECO:0000269|PubMed:9614189 |
| Chain | Residue | Details |
| D | SER262 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | MOD_RES: Deamidated asparagine; in tau and PHF-tau; partial => ECO:0000269|PubMed:1512244 |
| Chain | Residue | Details |
| D | PRO279 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 10 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 |
| Chain | Residue | Details |
| D | PRO281 | |
| D | THR388 | |
| D | LYS299 | |
| D | VAL312 | |
| D | ASN319 | |
| D | LYS323 | |
| D | GLN333 | |
| D | PRO345 | |
| D | LYS350 | |
| D | LYS372 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:8999860 |
| Chain | Residue | Details |
| D | LYS286 | |
| D | LYS355 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7706316 |
| Chain | Residue | Details |
| D | SER294 | |
| D | SER326 | |
| D | THR359 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:7706316, ECO:0000269|PubMed:8999860 |
| Chain | Residue | Details |
| D | ARG306 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P10637 |
| Chain | Residue | Details |
| D | VAL352 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637 |
| Chain | Residue | Details |
| D | LYS397 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by CK1 and PDPK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| D | PRO399 |
| site_id | SWS_FT_FI24 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; alternate => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:21327254 |
| Chain | Residue | Details |
| D | SER208 | |
| D | SER238 |
| site_id | SWS_FT_FI26 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300 |
| Chain | Residue | Details |
| D | LYS225 | |
| D | LYS234 | |
| D | LYS259 | |
| D | VAL280 | |
| D | PRO281 | |
| D | LYS350 | |
| D | ILE356 | |
| D | LYS372 |
| site_id | SWS_FT_FI27 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000269|PubMed:21327254 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau => ECO:0000269|PubMed:16443603 |
| Chain | Residue | Details |
| D | LYS254 | |
| D | VAL312 | |
| D | ILE356 |
| site_id | SWS_FT_FI29 |
| Number of Residues | 11 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637 |
| Chain | Residue | Details |
| D | LYS372 | |
| D | THR388 | |
| D | LYS259 | |
| D | PRO281 | |
| D | LYS299 | |
| D | ASN319 | |
| D | LYS323 | |
| D | GLN333 | |
| D | PRO345 | |
| D | LYS350 |
| site_id | SWS_FT_FI30 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637 |
| Chain | Residue | Details |
| D | LYS267 | |
| D | LEU378 |
