##gff-version 3 P10636 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1512244;Dbxref=PMID:1512244 P10636 UniProtKB Chain 2 758 . . . ID=PRO_0000072739;Note=Microtubule-associated protein tau P10636 UniProtKB Repeat 561 591 . . . Note=Tau/MAP 1;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU00824,ECO:0000305|PubMed:7706316;Dbxref=PMID:7706316 P10636 UniProtKB Repeat 592 622 . . . Note=Tau/MAP 2;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU00824,ECO:0000305|PubMed:7706316;Dbxref=PMID:7706316 P10636 UniProtKB Repeat 623 653 . . . Note=Tau/MAP 3;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU00824,ECO:0000305|PubMed:7706316;Dbxref=PMID:7706316 P10636 UniProtKB Repeat 654 685 . . . Note=Tau/MAP 4;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU00824,ECO:0000305|PubMed:7706316;Dbxref=PMID:7706316 P10636 UniProtKB Region 1 573 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Region 561 685 . . . Note=Microtubule-binding domain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7706316;Dbxref=PMID:7706316 P10636 UniProtKB Region 715 734 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 1 20 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 27 41 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 45 71 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 179 193 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 340 354 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 382 397 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 439 453 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 508 528 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Compositional bias 719 734 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P10636 UniProtKB Site 24 24 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 44 44 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 67 67 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 381 381 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 391 391 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 392 392 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 394 394 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 465 465 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 497 497 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 507 507 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 541 541 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 557 557 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 571 571 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 574 574 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 584 584 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 591 591 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 607 607 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 611 611 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 615 615 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 628 628 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 634 634 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 638 638 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 648 648 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 657 657 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 660 660 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 687 687 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 692 692 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 700 700 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 702 702 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 712 712 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Site 755 755 . . . Note=Not glycated;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1512244;Dbxref=PMID:1512244 P10636 UniProtKB Modified residue 18 18 . . . Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14999081;Dbxref=PMID:14999081 P10636 UniProtKB Modified residue 29 29 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 46 46 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19332 P10636 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19332 P10636 UniProtKB Modified residue 69 69 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 71 71 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19332 P10636 UniProtKB Modified residue 111 111 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine%3B by SGK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16982696;Dbxref=PMID:16982696 P10636 UniProtKB Modified residue 396 396 . . . Note=Phosphoserine%3B in PHF-tau;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1899488;Dbxref=PMID:1899488 P10636 UniProtKB Modified residue 470 470 . . . Note=Phosphothreonine%3B by PDPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9614189;Dbxref=PMID:9614189 P10636 UniProtKB Modified residue 472 472 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 480 480 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 480 480 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 484 484 . . . Note=Deamidated asparagine%3B in tau and PHF-tau%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1512244;Dbxref=PMID:1512244 P10636 UniProtKB Modified residue 486 486 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 492 492 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 498 498 . . . Note=Phosphothreonine%3B by PDPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15546861;Dbxref=PMID:15546861 P10636 UniProtKB Modified residue 502 502 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 508 508 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 512 512 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 514 514 . . . Note=Phosphotyrosine%3B by TTBK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923168;Dbxref=PMID:16923168 P10636 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine%3B by PDPK1 and TTBK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923168;Dbxref=PMID:16923168 P10636 UniProtKB Modified residue 516 516 . . . Note=Phosphoserine%3B by PDPK1 and TTBK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15546861,ECO:0000269|PubMed:16923168,ECO:0000269|PubMed:19451179,ECO:0000269|PubMed:9614189;Dbxref=PMID:15546861,PMID:16923168,PMID:19451179,PMID:9614189 P10636 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine%3B by CK1%2C PDPK1 and TTBK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=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;Dbxref=PMID:14761950,PMID:15546861,PMID:16923168,PMID:18220336,PMID:19451179,PMID:21327254,PMID:23186163,PMID:24275569,PMID:9614189 P10636 UniProtKB Modified residue 522 522 . . . Note=Phosphothreonine%3B by CK1 and PDPK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14761950,ECO:0000269|PubMed:15546861,ECO:0000269|PubMed:19451179;Dbxref=PMID:14761950,PMID:15546861,PMID:19451179 P10636 UniProtKB Modified residue 529 529 . . . Note=Phosphothreonine%3B by BRSK1%2C BRSK2%2C DYRK2 and PDPK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15546861,ECO:0000269|PubMed:18599021,ECO:0000269|PubMed:19451179,ECO:0000269|PubMed:21985311,ECO:0000269|PubMed:9614189;Dbxref=PMID:15546861,PMID:18599021,PMID:19451179,PMID:21985311,PMID:9614189 P10636 UniProtKB Modified residue 531 531 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15546861,ECO:0000269|PubMed:16443603,ECO:0000269|PubMed:19451179,ECO:0000269|PubMed:9614189;Dbxref=PMID:15546861,PMID:16443603,PMID:19451179,PMID:9614189 P10636 UniProtKB Modified residue 534 534 . . . Note=Phosphothreonine%3B by PDPK1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16443603,ECO:0000269|PubMed:19451179;Dbxref=PMID:16443603,PMID:19451179 P10636 UniProtKB Modified residue 542 542 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 548 548 . . . Note=Phosphothreonine%3B by GSK3-beta and PDPK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:14690523,ECO:0000269|PubMed:15546861,ECO:0000269|PubMed:16443603,ECO:0007744|PubMed:23186163;Dbxref=PMID:14690523,PMID:15546861,PMID:16443603,PMID:23186163 P10636 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine%3B by PDPK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15546861,ECO:0000269|PubMed:16443603,ECO:0000269|PubMed:9614189,ECO:0007744|PubMed:23186163;Dbxref=PMID:15546861,PMID:16443603,PMID:23186163,PMID:9614189 P10636 UniProtKB Modified residue 554 554 . . . Note=Phosphoserine%3B by PHK;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16443603,ECO:0000269|PubMed:8999860;Dbxref=PMID:16443603,PMID:8999860 P10636 UniProtKB Modified residue 576 576 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 576 576 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 579 579 . . . Note=Phosphoserine%3B by MARK1%2C MARK2%2C MARK3%2C MARK4%2C BRSK1%2C BRSK2 and PHK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=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;Dbxref=PMID:15546861,PMID:16443603,PMID:19451179,PMID:21985311,PMID:23666762,PMID:7706316,PMID:8999860,PMID:9614189 P10636 UniProtKB Modified residue 596 596 . . . Note=Deamidated asparagine%3B in tau and PHF-tau%3B partial;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1512244;Dbxref=PMID:1512244 P10636 UniProtKB Modified residue 598 598 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 602 602 . . . Note=Phosphoserine%3B by PHK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999860;Dbxref=PMID:8999860 P10636 UniProtKB Modified residue 607 607 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 610 610 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7706316;Dbxref=PMID:7706316 P10636 UniProtKB Modified residue 615 615 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 622 622 . . . Note=Phosphoserine%3B by PHK;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7706316,ECO:0000269|PubMed:8999860;Dbxref=PMID:7706316,PMID:8999860 P10636 UniProtKB Modified residue 628 628 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 628 628 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 634 634 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 638 638 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 641 641 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7706316;Dbxref=PMID:7706316 P10636 UniProtKB Modified residue 648 648 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 660 660 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 664 664 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 666 666 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 669 669 . . . Note=Phosphoserine%3B by PHK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8999860;Dbxref=PMID:8999860 P10636 UniProtKB Modified residue 673 673 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7706316;Dbxref=PMID:7706316 P10636 UniProtKB Modified residue 686 686 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 702 702 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 711 711 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 713 713 . . . Note=Phosphoserine%3B by CK1 and PDPK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=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;Dbxref=PMID:14761950,PMID:15546861,PMID:16443603,PMID:19451179,PMID:19690332,PMID:21327254,PMID:23186163,PMID:9614189 P10636 UniProtKB Modified residue 717 717 . . . Note=Phosphoserine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 P10636 UniProtKB Modified residue 720 720 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Modified residue 721 721 . . . Note=Phosphoserine%3B by CK1 and PDPK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:14761950,ECO:0000269|PubMed:15546861,ECO:0000269|PubMed:19451179,ECO:0000269|PubMed:21327254,ECO:0000269|PubMed:9614189,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:14761950,PMID:15546861,PMID:19451179,PMID:19690332,PMID:21327254,PMID:23186163,PMID:9614189 P10636 UniProtKB Modified residue 726 726 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15546861,ECO:0007744|PubMed:19690332;Dbxref=PMID:15546861,PMID:19690332 P10636 UniProtKB Modified residue 733 733 . . . Note=Phosphoserine%3B by CaMK2 and TTBK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923168;Dbxref=PMID:16923168 P10636 UniProtKB Modified residue 739 739 . . . Note=Phosphoserine%3B by PDPK1 and TTBK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16443603,ECO:0000269|PubMed:16923168,ECO:0000269|PubMed:19451179,ECO:0000269|PubMed:9614189;Dbxref=PMID:16443603,PMID:16923168,PMID:19451179,PMID:9614189 P10636 UniProtKB Modified residue 744 744 . . . Note=Phosphothreonine%3B by TTBK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16923168;Dbxref=PMID:16923168 P10636 UniProtKB Glycosylation 87 87 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 383 383 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 467 467 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 480 480 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 491 491 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 525 525 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21327254;Dbxref=PMID:21327254 P10636 UniProtKB Glycosylation 542 542 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 551 551 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 555 555 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21327254;Dbxref=PMID:21327254 P10636 UniProtKB Glycosylation 576 576 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 597 597 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 598 598 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 664 664 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 670 670 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 686 686 . . . Note=N-linked (Glc) (glycation) lysine%3B in PHF-tau%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9326300;Dbxref=PMID:9326300 P10636 UniProtKB Glycosylation 717 717 . . . Note=O-linked (GlcNAc) serine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21327254;Dbxref=PMID:21327254 P10636 UniProtKB Disulfide bond 608 639 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P10636 UniProtKB Cross-link 44 44 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 571 571 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B in PHF-tau;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16443603;Dbxref=PMID:16443603 P10636 UniProtKB Cross-link 576 576 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 584 584 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 598 598 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 615 615 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 628 628 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B in PHF-tau;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16443603;Dbxref=PMID:16443603 P10636 UniProtKB Cross-link 634 634 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 638 638 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 648 648 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 660 660 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 664 664 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 670 670 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B in PHF-tau;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16443603;Dbxref=PMID:16443603 P10636 UniProtKB Cross-link 686 686 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 692 692 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Cross-link 702 702 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10637 P10636 UniProtKB Alternative sequence 1 44 . . . ID=VSP_003175;Note=In isoform Tau-A. MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLK->MLRALQQRKR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:2516729;Dbxref=PMID:2516729 P10636 UniProtKB Alternative sequence 45 73 . . . ID=VSP_003176;Note=In isoform Tau-A%2C isoform Tau-D and isoform Fetal-tau. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:2498079,ECO:0000303|PubMed:2516729,ECO:0000303|PubMed:3131773,ECO:0000303|Ref.7;Dbxref=PMID:15489334,PMID:2498079,PMID:2516729,PMID:3131773 P10636 UniProtKB Alternative sequence 74 102 . . . ID=VSP_003177;Note=In isoform Tau-A%2C isoform Tau-B%2C isoform Tau-D%2C isoform Tau-E and isoform Fetal-tau. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:2484340,ECO:0000303|PubMed:2498079,ECO:0000303|PubMed:2516729,ECO:0000303|PubMed:3131773,ECO:0000303|Ref.6,ECO:0000303|Ref.7;Dbxref=PMID:15489334,PMID:2484340,PMID:2498079,PMID:2516729,PMID:3131773 P10636 UniProtKB Alternative sequence 103 104 . . . ID=VSP_003178;Note=In isoform Tau-A. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:2516729;Dbxref=PMID:2516729 P10636 UniProtKB Alternative sequence 125 375 . . . ID=VSP_003179;Note=In isoform Tau-A%2C isoform Tau-B%2C isoform Tau-C%2C isoform Tau-D%2C isoform Tau-E%2C isoform Tau-F and isoform Fetal-tau. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:2484340,ECO:0000303|PubMed:2498079,ECO:0000303|PubMed:2516729,ECO:0000303|PubMed:3131773,ECO:0000303|Ref.6,ECO:0000303|Ref.7;Dbxref=PMID:15489334,PMID:2484340,PMID:2498079,PMID:2516729,PMID:3131773 P10636 UniProtKB Alternative sequence 395 460 . . . ID=VSP_003180;Note=In isoform Tau-A%2C isoform Tau-B%2C isoform Tau-C%2C isoform Tau-D%2C isoform Tau-E%2C isoform Tau-F and isoform Fetal-tau. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:2484340,ECO:0000303|PubMed:2498079,ECO:0000303|PubMed:2516729,ECO:0000303|PubMed:3131773,ECO:0000303|Ref.6,ECO:0000303|Ref.7;Dbxref=PMID:15489334,PMID:2484340,PMID:2498079,PMID:2516729,PMID:3131773 P10636 UniProtKB Alternative sequence 502 502 . . . ID=VSP_026780;Note=In isoform Tau-G. S->SATKQVQRRPPPAGPRSER;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10636 UniProtKB Alternative sequence 592 622 . . . ID=VSP_003181;Note=In isoform Tau-A%2C isoform Tau-B%2C isoform Tau-C and isoform Fetal-tau. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:2484340,ECO:0000303|PubMed:2516729,ECO:0000303|PubMed:3131773,ECO:0000303|Ref.7;Dbxref=PMID:15489334,PMID:2484340,PMID:2516729,PMID:3131773 P10636 UniProtKB Natural variant 5 5 . . . ID=VAR_019660;Note=In FTD%3B reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11921059;Dbxref=dbSNP:rs63750959,PMID:11921059 P10636 UniProtKB Natural variant 5 5 . . . ID=VAR_019661;Note=In PSNP1%3B delays assembly initiation and lowers the mass of microtubules formed%3B but the assembly rate is increased compared to normal tau. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12325083;Dbxref=dbSNP:rs63750959,PMID:12325083 P10636 UniProtKB Natural variant 17 17 . . . ID=VAR_064622;Note=T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20020531;Dbxref=dbSNP:rs144611688,PMID:20020531 P10636 UniProtKB Natural variant 30 30 . . . ID=VAR_064623;Note=T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20020531;Dbxref=dbSNP:rs748728879,PMID:20020531 P10636 UniProtKB Natural variant 285 285 . . . ID=VAR_010340;Note=Risk factor for PSNP1. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10534245,ECO:0000269|PubMed:9629852;Dbxref=dbSNP:rs62063786,PMID:10534245,PMID:9629852 P10636 UniProtKB Natural variant 289 289 . . . ID=VAR_010341;Note=Risk factor for PSNP1. V->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10534245,ECO:0000269|PubMed:9629852;Dbxref=dbSNP:rs62063787,PMID:10534245,PMID:9629852 P10636 UniProtKB Natural variant 370 370 . . . ID=VAR_056121;Note=R->W;Dbxref=dbSNP:rs17651549 P10636 UniProtKB Natural variant 441 441 . . . ID=VAR_010342;Note=Y->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1420178,ECO:0000269|PubMed:15365985,ECO:0000269|PubMed:9629852;Dbxref=dbSNP:rs2258689,PMID:1420178,PMID:15365985,PMID:9629852 P10636 UniProtKB Natural variant 447 447 . . . ID=VAR_010343;Note=S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9629852;Dbxref=dbSNP:rs10445337,PMID:9629852 P10636 UniProtKB Natural variant 574 574 . . . ID=VAR_010344;Note=In PIDB%3B reduces the ability to promote microtubule assembly by 70%25. K->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11089577,ECO:0000269|PubMed:11117542;Dbxref=dbSNP:rs63750129,PMID:11089577,PMID:11117542 P10636 UniProtKB Natural variant 583 583 . . . ID=VAR_019662;Note=In FTD%3B less able to promote microtubule assembly than wild-type tau. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12509859;Dbxref=dbSNP:rs63750349,PMID:12509859 P10636 UniProtKB Natural variant 589 589 . . . ID=VAR_010345;Note=In FTD. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9641683,ECO:0000269|PubMed:9973279;Dbxref=dbSNP:rs63750376,PMID:9641683,PMID:9973279 P10636 UniProtKB Natural variant 590 590 . . . ID=VAR_084361;Note=In FTD%3B increased aggregation propensity and altered binding affinity towards microtubules and F-actin. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32961270;Dbxref=dbSNP:rs1247408229,PMID:32961270 P10636 UniProtKB Natural variant 596 596 . . . ID=VAR_010346;Note=In FTD%3B with parkinsonism. N->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10412802,ECO:0000269|PubMed:10489057,ECO:0000269|PubMed:10802785,ECO:0000269|PubMed:12473774,ECO:0000269|PubMed:9789048;Dbxref=dbSNP:rs63750756,PMID:10412802,PMID:10489057,PMID:10802785,PMID:12473774,PMID:9789048 P10636 UniProtKB Natural variant 597 597 . . . ID=VAR_010347;Note=In FTD. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9973279;Dbxref=dbSNP:rs63750688,PMID:9973279 P10636 UniProtKB Natural variant 613 613 . . . ID=VAR_019663;Note=In FTD%3B reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation%3B effects at both the RNA and the protein level. N->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11585254,ECO:0000269|PubMed:11906000;Dbxref=dbSNP:rs63750416,PMID:11585254,PMID:11906000 P10636 UniProtKB Natural variant 613 613 . . . ID=VAR_019664;Note=In PSNP1/atypical PSNP1%3B heterozygosity may be a risk factor for both a PSNP1-like syndrome and Parkinson disease%3B reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation%3B effects at both the RNA and the protein level. Missing;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11220749,ECO:0000269|PubMed:11906000,ECO:0000269|PubMed:14991828,ECO:0000269|PubMed:14991829;Dbxref=PMID:11220749,PMID:11906000,PMID:14991828,PMID:14991829 P10636 UniProtKB Natural variant 617 617 . . . ID=VAR_064624;Note=V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20020531;Dbxref=dbSNP:rs116733906,PMID:20020531 P10636 UniProtKB Natural variant 618 618 . . . ID=VAR_010348;Note=In FTD%3B most common mutation%3B reduction in the ability to promote microtubule assembly%3B accelerates aggregation of tau into filaments. P->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10214944,ECO:0000269|PubMed:9641683,ECO:0000269|PubMed:9736786,ECO:0000269|PubMed:9789048,ECO:0000269|PubMed:9973279;Dbxref=dbSNP:rs63751273,PMID:10214944,PMID:9641683,PMID:9736786,PMID:9789048,PMID:9973279 P10636 UniProtKB Natural variant 618 618 . . . ID=VAR_010349;Note=In FTD and CBD%3B reduction in the ability to promote microtubule assembly. P->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10374757,ECO:0000269|PubMed:10553987,ECO:0000269|PubMed:11071507,ECO:0000269|PubMed:16240366;Dbxref=dbSNP:rs63751438,PMID:10374757,PMID:10553987,PMID:11071507,PMID:16240366 P10636 UniProtKB Natural variant 620 620 . . . ID=VAR_037439;Note=In PSNP1. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16157753;Dbxref=dbSNP:rs63751391,PMID:16157753 P10636 UniProtKB Natural variant 622 622 . . . ID=VAR_010350;Note=In FTD%3B minimal parkinsonism%3B very early age of onset. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10208578;Dbxref=dbSNP:rs63751165,PMID:10208578 P10636 UniProtKB Natural variant 634 634 . . . ID=VAR_037440;Note=In FTD. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15883319;Dbxref=dbSNP:rs63750092,PMID:15883319 P10636 UniProtKB Natural variant 637 637 . . . ID=VAR_019665;Note=In PIDB%3B markedly reduced ability of tau to promote microtubule assembly. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11891833;Dbxref=dbSNP:rs63750635,PMID:11891833 P10636 UniProtKB Natural variant 654 654 . . . ID=VAR_010351;Note=In FTD%3B ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease%3B accelerates aggregation of tau into filaments. V->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10214944,ECO:0000269|PubMed:9629852;Dbxref=dbSNP:rs63750570,PMID:10214944,PMID:9629852 P10636 UniProtKB Natural variant 659 659 . . . ID=VAR_019666;Note=In FTD. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11117541;Dbxref=dbSNP:rs63750711,PMID:11117541 P10636 UniProtKB Natural variant 669 669 . . . ID=VAR_019667;Note=In fatal respiratory hypoventilation%3B unusual apparent autosomal recessive inheritance%3B reduced binding to microtubules as well as increased fibrillization and aggregation. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14595660;Dbxref=dbSNP:rs63750425,PMID:14595660 P10636 UniProtKB Natural variant 686 686 . . . ID=VAR_019668;Note=In PIDB%3B 90%25 reduction in the rate of microtubule assembly. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11601501;Dbxref=dbSNP:rs63751264,PMID:11601501 P10636 UniProtKB Natural variant 706 706 . . . ID=VAR_010352;Note=In PIDB%3B in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%25. G->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10604746,ECO:0000269|PubMed:11117542;Dbxref=dbSNP:rs63750512,PMID:10604746,PMID:11117542 P10636 UniProtKB Natural variant 723 723 . . . ID=VAR_010353;Note=In FTD/Alzheimer disease%3B accelerates aggregation of tau into filaments%3B reduces tau phosphorylation in cells compared to both the wild-type and other mutant forms. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10214944,ECO:0000269|PubMed:11278002,ECO:0000269|PubMed:11889249,ECO:0000269|PubMed:14517953,ECO:0000269|PubMed:26086902,ECO:0000269|PubMed:9641683,ECO:0000269|PubMed:9973279;Dbxref=dbSNP:rs63750424,PMID:10214944,PMID:11278002,PMID:11889249,PMID:14517953,PMID:26086902,PMID:9641683,PMID:9973279 P10636 UniProtKB Mutagenesis 515 515 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Mutagenesis 516 516 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Mutagenesis 519 519 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Mutagenesis 531 531 . . . Note=No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein. S->A P10636 UniProtKB Mutagenesis 548 548 . . . Note=50%25 Decrease in microtubule-binding after in vitro phosphorylation of mutant protein. T->A P10636 UniProtKB Mutagenesis 548 548 . . . Note=No association with plasma membrane. T->E P10636 UniProtKB Mutagenesis 552 552 . . . Note=70%25 decrease in microtubule-binding after in vitro phosphorylation of mutant protein. S->A P10636 UniProtKB Mutagenesis 552 552 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Mutagenesis 579 579 . . . Note=8%25 decrease in microtubule-binding after in vitro phosphorylation of mutant protein. S->A P10636 UniProtKB Mutagenesis 713 713 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Mutagenesis 721 721 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Mutagenesis 726 726 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Mutagenesis 730 730 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Mutagenesis 739 739 . . . Note=No association with plasma membrane. S->E P10636 UniProtKB Sequence conflict 48 48 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10636 UniProtKB Sequence conflict 414 414 . . . Note=H->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10636 UniProtKB Sequence conflict 557 557 . . . Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10636 UniProtKB Sequence conflict 591 591 . . . Note=K->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10636 UniProtKB Sequence conflict 617 617 . . . Note=V->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10636 UniProtKB Sequence conflict 622 622 . . . Note=S->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 P10636 UniProtKB Beta strand 7 9 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6N4P P10636 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZV3 P10636 UniProtKB Turn 63 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZV3 P10636 UniProtKB Turn 579 582 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6CVJ P10636 UniProtKB Beta strand 587 590 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5N5A P10636 UniProtKB Beta strand 592 610 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P6A P10636 UniProtKB Beta strand 613 615 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QK6 P10636 UniProtKB Beta strand 618 620 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MP5 P10636 UniProtKB Turn 622 624 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5N5B P10636 UniProtKB Beta strand 625 627 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4E0N P10636 UniProtKB Beta strand 629 631 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QKZ P10636 UniProtKB Beta strand 634 640 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P6A P10636 UniProtKB Beta strand 645 647 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P6A P10636 UniProtKB Beta strand 654 657 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P6A P10636 UniProtKB Beta strand 660 663 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P6A P10636 UniProtKB Beta strand 666 671 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P6A P10636 UniProtKB Beta strand 674 679 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P6A P10636 UniProtKB Beta strand 682 684 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7P6A P10636 UniProtKB Beta strand 686 693 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8ORF P10636 UniProtKB Beta strand 694 706 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QKY P10636 UniProtKB Beta strand 709 712 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QKY P10636 UniProtKB Beta strand 716 720 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SP1 P10636 UniProtKB Beta strand 723 732 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QKY P10636 UniProtKB Beta strand 734 738 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QKY P10636 UniProtKB Beta strand 741 751 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QKY P10636 UniProtKB Beta strand 753 755 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QKY