eF-site ID 5o3l-F PDB Code 5o3l Chain F click to enlarge Title Paired helical filament in Alzheimer's disease brain Classification STRUCTURAL PROTEIN Compound Microtubule-associated protein tau Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence F:  VQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLD FKDRVQSKIGSLDNITHVPGGGNKKIETHKLTF Description (1)  Microtubule-associated protein tau Functional site 1) chain F residue 311 type SITE sequence K description Not glycated => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI1 2) chain F residue 317 type SITE sequence K description Not glycated => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI1 3) chain F residue 321 type SITE sequence K description Not glycated => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI1 4) chain F residue 331 type SITE sequence K description Not glycated => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI1 5) chain F residue 340 type SITE sequence K description Not glycated => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI1 6) chain F residue 343 type SITE sequence K description Not glycated => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI1 7) chain F residue 370 type SITE sequence K description Not glycated => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI1 8) chain F residue 375 type SITE sequence K description Not glycated => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI1 9) chain F residue 311 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI2 10) chain F residue 317 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI2 11) chain F residue 321 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI2 12) chain F residue 331 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI2 13) chain F residue 343 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI2 14) chain F residue 347 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI2 15) chain F residue 369 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI2 16) chain F residue 324 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:7706316 source Swiss-Prot : SWS_FT_FI3 17) chain F residue 356 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:7706316 source Swiss-Prot : SWS_FT_FI3 18) chain F residue 349 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI4 19) chain F residue 352 type MOD_RES sequence S description Phosphoserine; by PHK => ECO:0000269|PubMed:8999860 source Swiss-Prot : SWS_FT_FI5 20) chain F residue 347 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI6 21) chain F residue 353 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI6 22) chain F residue 369 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300 source Swiss-Prot : SWS_FT_FI6 23) chain F residue 311 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI7 24) chain F residue 353 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau => ECO:0000269|PubMed:16443603 source Swiss-Prot : SWS_FT_FI7 25) chain F residue 375 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI8 26) chain F residue 317 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI9 27) chain F residue 321 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI9 28) chain F residue 331 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI9 29) chain F residue 343 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI9 30) chain F residue 347 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI9 31) chain F residue 369 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links