6CVN
Model of synthetic tau (R2x4) bound to the microtubule
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0005515 | molecular_function | protein binding |
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 | 0046872 | molecular_function | metal ion 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 | 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 | 0015630 | cellular_component | microtubule cytoskeleton |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion 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 | 13 |
Details | binding site for residue GDP A 501 |
Chain | Residue |
A | GLN11 |
A | ASP179 |
A | ASN206 |
A | TYR224 |
A | ASN228 |
A | CYS12 |
A | GLN15 |
A | ASN101 |
A | SER140 |
A | GLY143 |
A | GLY144 |
A | THR145 |
A | GLY146 |
site_id | AC2 |
Number of Residues | 21 |
Details | binding site for residue GTP B 501 |
Chain | Residue |
A | LYS254 |
B | GLY10 |
B | GLN11 |
B | ALA12 |
B | GLN15 |
B | ALA99 |
B | ALA100 |
B | ASN101 |
B | SER140 |
B | GLY143 |
B | GLY144 |
B | THR145 |
B | GLY146 |
B | ILE171 |
B | THR179 |
B | GLU183 |
B | ASN206 |
B | TYR224 |
B | LEU227 |
B | ASN228 |
B | MG502 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue MG B 502 |
Chain | Residue |
B | GTP501 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue GDP C 501 |
Chain | Residue |
C | GLN11 |
C | CYS12 |
C | GLN15 |
C | ILE16 |
C | ASN101 |
C | SER140 |
C | GLY143 |
C | GLY144 |
C | THR145 |
C | GLY146 |
C | ASP179 |
C | ASN206 |
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 |
B | GLY142-GLY148 | |
A | GLY142-GLY148 |
site_id | PS00228 |
Number of Residues | 4 |
Details | TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI |
Chain | Residue | Details |
A | MET1-ILE4 |
site_id | PS00229 |
Number of Residues | 13 |
Details | TAU_MAP_1 Tau and MAP proteins tubulin-binding repeat signature. GSkdNikHvPGGG |
Chain | Residue | Details |
D | GLY261-GLY273 | |
D | GLY292-GLY304 | |
D | GLY323-GLY335 | |
D | GLY354-GLY366 |
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 | LYS225 | |
D | LYS312 | |
D | VAL318 | |
D | CYS322 | |
D | PRO332 | |
D | ASN341 | |
D | LEU344 | |
D | GLU371 | |
D | THR376 | |
D | LYS384 | |
D | ASP386 | |
D | LYS241 | |
D | PRO396 | |
D | ASN255 | |
D | SER258 | |
D | HIS268 | |
D | VAL275 | |
D | CYS291 | |
D | ASP295 | |
D | HIS299 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by TTBK1 => ECO:0000269|PubMed:16923168 |
Chain | Residue | Details |
D | TYR198 | |
B | GLU71 | |
B | SER140 | |
B | GLY144 | |
B | THR145 | |
B | THR179 | |
B | ASN206 | |
B | 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 | SER199 | |
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 | SER200 | |
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 | SER203 | |
B | SER232 |
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 | THR206 | |
A | 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 | THR213 | |
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 | SER215 | |
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 | THR218 | |
C | LYS60 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10637 |
Chain | Residue | Details |
D | LYS226 | |
D | CYS291 | |
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 | THR232 |
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 | SER236 | |
B | 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 | SER238 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P10637 |
Chain | Residue | Details |
D | CYS260 |
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 | LYS263 |
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 | LYS280 |
site_id | SWS_FT_FI17 |
Number of Residues | 10 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 |
Chain | Residue | Details |
D | LEU282 | |
D | ASP386 | |
D | HIS299 | |
D | LYS312 | |
D | VAL318 | |
D | CYS322 | |
D | PRO332 | |
D | LEU344 | |
D | ASN348 | |
D | ILE370 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:8999860 |
Chain | Residue | Details |
D | ASN286 | |
D | CYS353 |
site_id | SWS_FT_FI19 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7706316 |
Chain | Residue | Details |
D | LYS294 | |
D | LYS325 | |
D | ASP357 |
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 | VAL306 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P10637 |
Chain | Residue | Details |
D | GLN350 |
site_id | SWS_FT_FI22 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637 |
Chain | Residue | Details |
D | SER395 |
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 | VAL397 |
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 | SER209 | |
D | SER239 |
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 | LYS226 | |
D | LYS235 | |
D | CYS260 | |
D | LYS281 | |
D | LEU282 | |
D | ASN348 | |
D | GLY354 | |
D | ILE370 |
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 | ASN255 | |
D | LYS312 | |
D | GLY354 |
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 | ILE370 | |
D | ASP386 | |
D | CYS260 | |
D | LEU282 | |
D | HIS299 | |
D | VAL318 | |
D | CYS322 | |
D | PRO332 | |
D | LEU344 | |
D | ASN348 |
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 | HIS268 | |
D | THR376 |