Variant position: 596 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 758 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human KIGSTENLKHQPGGGKVQII NKKLDLSNVQSKCGSKDNIKH
Gorilla KIGSTENLKHQPGGGKVQII NKKLDLSNVQSKCGSKDNIKH
Rhesus macaque KIGSTENLKHQPGGGKVQII NKKLDLSNVQSKCGSKDNIKH
Chimpanzee KIGSTENLKHQPGGGKVQII NKKLDLSNVQSKCGSKDNIKH
Mouse KIGSTENLKHQPGGGKVQII NKKLDLSNVQSKCGSKDNIKH
Rat KIGSTENLKHQPGGGKVQII NKKLDLSNVQSKCGSKDNIKH
Bovine KIGSTENLKHQPGGGKVQII NKKLDLSNVQSKCGSKDNIKH
Goat KIGSTENLKHQPGGGKVQII NKKLDLSNVQSKCGSKDNIKH
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
2 – 758 Microtubule-associated protein tau
592 – 622 Tau/MAP 2
584 – 584 Not glycated
591 – 591 Not glycated
607 – 607 Not glycated
611 – 611 Not glycated
615 – 615 Not glycated
579 – 579 Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK
596 – 596 Deamidated asparagine; in tau and PHF-tau; partial
602 – 602 Phosphoserine; by PHK
606 – 606 Phosphoserine; by PHK
610 – 610 Phosphoserine; by MARK1; in PHF-tau
576 – 576 N-linked (Glc) (glycation); in PHF-tau; in vitro
597 – 597 N-linked (Glc) (glycation); in PHF-tau; in vitro
598 – 598 N-linked (Glc) (glycation); in PHF-tau; in vitro
592 – 622 Missing. In isoform Tau-A, isoform Tau-B, isoform Tau-C and isoform Fetal-tau.
579 – 579 S -> A. 8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
No reference for the current variant in UniProtKB/Swiss-Prot.
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.