P10636 (TAU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Microtubule-associated protein tau

Alternative name(s):
Neurofibrillary tangle protein
Paired helical filament-tau
Short name=PHF-tau

Gene names

Name:	MAPT
Synonyms:	MAPTL, MTBT1, TAU

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	758 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
Subunit structure	Interacts with PSMC2 through SQSTM1 By similarity. Interacts with SQSTM1 when polyubiquitinated. Interacts with FKBP4 By similarity. Binds to CSNK1D. Interacts with SGK1. Ref.24 Ref.28 Ref.31
Subcellular location	Cytoplasm › cytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Cell projection › axon. Note: Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components. Ref.23
Tissue specificity	Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.
Developmental stage	Four-repeat (type II) tau is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) tau is found in both adult and fetal brain.
Domain	The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.
Post-translational modification	Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1: CDK1, CDK5, GSK3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in the form associated with paired helical filaments (PHF-tau)), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly. Phosphorylation decreases with age. Phosphorylation within tau's repeat domain or in flanking regions seems to reduce tau's interaction with, respectively, microtubules or plasma membrane components. Phosphorylation on Ser-610, Ser-622, Ser-641 and Ser-673 in several isoforms during mitosis. Phosphorylation at Ser-548 by GSK3B reduces ability to bind and stabilize microtubules. Phosphorylation at Ser-579 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated at Ser-554, Ser-579, Ser-602, Ser-606 and Ser-669 by PHK. Phosphorylation at Ser-214 by SGK1 mediates microtubule depolymerization and neurite formation in hippocampal neurons. Ref.13 Ref.14 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome By similarity. PHF-tau can be modified by three different forms of polyubiquitination. 'Lys-48'-linked polyubiquitination is the major form, 'Lys-6'-linked and 'Lys-11'-linked polyubiquitination also occur. Glycation of PHF-tau, but not normal brain tau. Glycation is a non-enzymatic post-translational modification that involves a covalent linkage between a sugar and an amino group of a protein molecule forming ketoamine. Subsequent oxidation, fragmentation and/or cross-linking of ketoamine leads to the production of advanced glycation endproducts (AGES). Glycation may play a role in stabilizing PHF aggregation leading to tangle formation in AD.
Involvement in disease	Note=In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments (PHF) and straight filaments, mainly composed of hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU). Ref.71 Defects in MAPT are a cause of frontotemporal dementia (FTD) [MIM:600274]; also called frontotemporal dementia (FTD), pallido-ponto-nigral degeneration (PPND) or historically termed Pick complex. This form of frontotemporal dementia is characterized by presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons. Ref.40 Ref.42 Ref.43 Ref.44 Ref.46 Ref.47 Ref.48 Ref.49 Ref.51 Ref.53 Ref.54 Ref.57 Ref.58 Ref.59 Ref.62 Ref.63 Ref.65 Ref.67 Ref.68 Ref.69 Ref.71 Ref.74 Ref.76 Defects in MAPT are a cause of Pick disease of the brain (PIDB) [MIM:172700]. It is a rare form of dementia pathologically defined by severe atrophy, neuronal loss and gliosis. It is characterized by the occurrence of tau-positive inclusions, swollen neurons (Pick cells) and argentophilic neuronal inclusions known as Pick bodies that disproportionally affect the frontal and temporal cortical regions. Clinical features include aphasia, apraxia, confusion, anomia, memory loss and personality deterioration. Ref.50 Ref.55 Ref.56 Ref.61 Ref.64 Ref.71 Note=Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease. Ref.71 Defects in MAPT are a cause of progressive supranuclear palsy type 1 (PSNP1) [MIM:601104]; also abbreviated as PSP and also known as Steele-Richardson-Olszewski syndrome. PSNP1 is characterized by akinetic-rigid syndrome, supranuclear gaze palsy, pyramidal tract dysfunction, pseudobulbar signs and cognitive capacities deterioration. Neurofibrillary tangles and gliosis but no amyloid plaques are found in diseased brains. Most cases appear to be sporadic, with a significant association with a common haplotype including the MAPT gene and the flanking regions. Familial cases show an autosomal dominant pattern of transmission with incomplete penetrance; genetic analysis of a few cases showed the occurrence of tau mutations, including a deletion of Asn-613. Ref.52 Ref.60 Ref.66 Ref.71 Ref.72 Ref.73 Ref.75 Defects in MAPT are a cause of Parkinson-dementia syndrome (PARDE) [MIM:260540]. A syndrome characterized by parkinsonism tremor, rigidity, dementia, ophthalmoparesis and pyramidal signs. Neurofibrillary degeneration occurs in the hippocampus, basal ganglia and brainstem nuclei. Ref.71
Sequence similarities	Contains 4 Tau/MAP repeats.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Alzheimer disease Disease mutation Neurodegeneration Parkinsonism
Domain	Repeat
PTM	Acetylation Disulfide bond Glycation Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular component disassembly involved in apoptosis Traceable author statement. Source: Reactome microtubule cytoskeleton organization Inferred from direct assay. Source: UniProtKB negative regulation of microtubule depolymerization Inferred from electronic annotation. Source: InterPro positive regulation of axon extension Inferred from direct assay. Source: UniProtKB positive regulation of microtubule polymerization Inferred from direct assay. Source: UniProtKB regulation of autophagy Inferred from genetic interaction. Source: MGI
Cellular component	axon Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome growth cone Inferred from direct assay. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Traceable author statement. Source: ProtInc nuclear periphery Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay. Source: UniProtKB tubulin complex Inferred from direct assay. Source: UniProtKB
Molecular function	SH3 domain binding Inferred from physical interaction. Source: UniProtKB apolipoprotein E binding Inferred from physical interaction. Source: BHF-UCL enzyme binding Inferred from physical interaction. Source: UniProtKB lipoprotein particle binding Inferred from physical interaction. Source: UniProtKB microtubule binding Inferred from direct assay. Source: UniProtKB structural constituent of cytoskeleton Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	9	EBI-366182,EBI-77613
STUB1	Q9UNE7	2	EBI-366182,EBI-357085

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Isoforms differ from each other by the presence or absence of up to 5 of the 15 exons. One of these optional exons contains the additional tau/MAP repeat.

Isoform PNS-tau (identifier: P10636-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Fetal-tau (identifier: P10636-2)

The sequence of this isoform differs from the canonical sequence as follows:
     45-73: Missing.
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.

Isoform Tau-A (identifier: P10636-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLK → MLRALQQRKR
     45-73: Missing.
     74-102: Missing.
     103-104: Missing.
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.

Isoform Tau-B (identifier: P10636-4)

The sequence of this isoform differs from the canonical sequence as follows:
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.

Isoform Tau-C (identifier: P10636-5)

Also known as: Tau-3;

The sequence of this isoform differs from the canonical sequence as follows:
     125-375: Missing.
     395-460: Missing.
     592-622: Missing.

Isoform Tau-D (identifier: P10636-6)

The sequence of this isoform differs from the canonical sequence as follows:
     45-73: Missing.
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.

Isoform Tau-E (identifier: P10636-7)

The sequence of this isoform differs from the canonical sequence as follows:
     74-102: Missing.
     125-375: Missing.
     395-460: Missing.

Isoform Tau-F (identifier: P10636-8)

Also known as: Tau-4;

The sequence of this isoform differs from the canonical sequence as follows:
     125-375: Missing.
     395-460: Missing.

Isoform Tau-G (identifier: P10636-9)

The sequence of this isoform differs from the canonical sequence as follows:
     502-502: S → SATKQVQRRPPPAGPRSER

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.10
	Chain	2 – 758	757	Microtubule-associated protein tau		PRO_0000072739
Regions
	Repeat	561 – 591	31	Tau/MAP 1
	Repeat	592 – 622	31	Tau/MAP 2
	Repeat	623 – 653	31	Tau/MAP 3
	Repeat	654 – 685	32	Tau/MAP 4
Sites
	Site	24	1	Not glycated
	Site	44	1	Not glycated
	Site	67	1	Not glycated
	Site	381	1	Not glycated
	Site	391	1	Not glycated
	Site	392	1	Not glycated
	Site	394	1	Not glycated
	Site	465	1	Not glycated
	Site	497	1	Not glycated
	Site	507	1	Not glycated
	Site	541	1	Not glycated
	Site	557	1	Not glycated
	Site	571	1	Not glycated
	Site	574	1	Not glycated
	Site	584	1	Not glycated
	Site	591	1	Not glycated
	Site	607	1	Not glycated
	Site	611	1	Not glycated
	Site	615	1	Not glycated
	Site	628	1	Not glycated
	Site	634	1	Not glycated
	Site	638	1	Not glycated
	Site	648	1	Not glycated
	Site	657	1	Not glycated
	Site	660	1	Not glycated
	Site	687	1	Not glycated
	Site	692	1	Not glycated
	Site	700	1	Not glycated
	Site	702	1	Not glycated
	Site	712	1	Not glycated
	Site	755	1	Not glycated
Amino acid modifications
	Modified residue	2	1	N-acetylalanine
	Modified residue	46	1	Phosphoserine; by PDPK1
	Modified residue	50	1	Phosphothreonine; by PDPK1
	Modified residue	111	1	Phosphothreonine By similarity
	Modified residue	214	1	Phosphoserine; by SGK1 Ref.31
	Modified residue	470	1	Phosphothreonine; by PDPK1
	Modified residue	484	1	Deamidated asparagine; in tau and PHF-tau; partial
	Modified residue	492	1	Phosphothreonine; by PDPK1
	Modified residue	498	1	Phosphothreonine; by PDPK1
	Modified residue	514	1	Phosphotyrosine; by TTBK1 Ref.30
	Modified residue	515	1	Phosphoserine; by PDPK1 and TTBK1 Ref.30
	Modified residue	516	1	Phosphoserine; by PDPK1 and TTBK1 Ref.30 Ref.36
	Modified residue	519	1	Phosphoserine; by CK1, PDPK1 and TTBK1 Ref.24 Ref.27 Ref.29 Ref.30 Ref.35 Ref.36 Ref.37
	Modified residue	522	1	Phosphothreonine; by CK1 and PDPK1 Ref.24 Ref.36
	Modified residue	529	1	Phosphothreonine; by PDPK1 Ref.33 Ref.35
	Modified residue	531	1	Phosphoserine; by PKA Ref.13
	Modified residue	534	1	Phosphothreonine; by PDPK1 Ref.13 Ref.35
	Modified residue	548	1	Phosphothreonine; by GSK3-beta and PDPK1 Ref.13 Ref.25 Ref.29 Ref.34
	Modified residue	552	1	Phosphoserine; by PDPK1 Ref.13 Ref.34
	Modified residue	554	1	Phosphoserine; by PHK Ref.13 Ref.19
	Modified residue	579	1	Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK Ref.13 Ref.19 Ref.36
	Modified residue	596	1	Deamidated asparagine; in tau and PHF-tau; partial
	Modified residue	602	1	Phosphoserine; by PHK Ref.19
	Modified residue	606	1	Phosphoserine; by PHK Ref.19
	Modified residue	610	1	Phosphoserine; by MARK1; in PHF-tau
	Modified residue	622	1	Phosphoserine; by MARK1; in PHF-tau
	Modified residue	641	1	Phosphoserine; by MARK1; in PHF-tau
	Modified residue	669	1	Phosphoserine; by PHK Ref.19
	Modified residue	673	1	Phosphoserine; by MARK1; in PHF-tau Ref.29
	Modified residue	713	1	Phosphoserine; by CK1 and PDPK1 Ref.13 Ref.24 Ref.29 Ref.37
	Modified residue	717	1	Phosphoserine Ref.36 Ref.37
	Modified residue	720	1	Phosphothreonine Ref.29
	Modified residue	721	1	Phosphoserine; by CK1 and PDPK1 Ref.24 Ref.29 Ref.35 Ref.36 Ref.37
	Modified residue	726	1	Phosphoserine Ref.37
	Modified residue	729	1	Phosphoserine By similarity
	Modified residue	731	1	Phosphothreonine By similarity
	Modified residue	733	1	Phosphoserine; by CaMK2 and TTBK1 Ref.30
	Modified residue	739	1	Phosphoserine; by PDPK1 and TTBK1 Ref.13 Ref.30
	Modified residue	744	1	Phosphothreonine; by TTBK1 Ref.30
	Glycosylation	87	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	383	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	467	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	480	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	491	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	542	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	551	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	576	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	597	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	598	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	664	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	670	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Glycosylation	686	1	N-linked (Glc) (glycation); in PHF-tau; in vitro Ref.20
	Disulfide bond	608 ↔ 639		By similarity
	Cross-link	571		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau Ref.13
	Cross-link	628		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau Ref.13
	Cross-link	670		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau Ref.13
Natural variations
	Alternative sequence	1 – 44	44	MAEPR…DAGLK → MLRALQQRKR in isoform Tau-A.		VSP_003175
	Alternative sequence	45 – 73	29	Missing in isoform Tau-A, isoform Tau-D and isoform Fetal-tau.		VSP_003176
	Alternative sequence	74 – 102	29	Missing in isoform Tau-A, isoform Tau-B, isoform Tau-D, isoform Tau-E and isoform Fetal-tau.		VSP_003177
	Alternative sequence	103 – 104	2	Missing in isoform Tau-A.		VSP_003178
	Alternative sequence	125 – 375	251	Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Fetal-tau.		VSP_003179
	Alternative sequence	395 – 460	66	Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Fetal-tau.		VSP_003180
	Alternative sequence	502	1	S → SATKQVQRRPPPAGPRSER in isoform Tau-G.		VSP_026780
	Alternative sequence	592 – 622	31	Missing in isoform Tau-A, isoform Tau-B, isoform Tau-C and isoform Fetal-tau.		VSP_003181
	Natural variant	5	1	R → H in FTD; reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro. Ref.65		VAR_019660
	Natural variant	5	1	R → L in PSNP1; delays assembly initiation and lowers the mass of microtubules formed; but the assembly rate is increased compared to normal tau. Ref.66		VAR_019661
	Natural variant	17	1	T → M. Ref.77		VAR_064622
	Natural variant	30	1	T → A. Ref.77		VAR_064623
	Natural variant	285	1	D → N Risk factor for PSNP1. Ref.40 Ref.52		VAR_010340
	Natural variant	289	1	V → A Risk factor for PSNP1. Ref.40 Ref.52		VAR_010341
	Natural variant	370	1	R → W. Corresponds to variant rs17651549 [ dbSNP | Ensembl ].		VAR_056121
	Natural variant	441	1	Y → H. Ref.5 Ref.17 Ref.40 Corresponds to variant rs2258689 [ dbSNP | Ensembl ].		VAR_010342
	Natural variant	447	1	S → P. Ref.40 Corresponds to variant rs10445337 [ dbSNP | Ensembl ].		VAR_010343
	Natural variant	574	1	K → T in PIDB; reduces the ability to promote microtubule assembly by 70%. Ref.55 Ref.56		VAR_010344
	Natural variant	583	1	L → V in FTD; less able to promote microtubule assembly than wild-type tau. Ref.69		VAR_019662
	Natural variant	589	1	G → V in FTD. Ref.43 Ref.46		VAR_010345
	Natural variant	596	1	N → K in FTD; with parkinsonism. Ref.44 Ref.45 Ref.51 Ref.57 Ref.63		VAR_010346
	Natural variant	597	1	Missing in FTD.		VAR_010347
	Natural variant	613	1	N → H in FTD; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level. Ref.59 Ref.67		VAR_019663
	Natural variant	613	1	Missing in PSNP1/atypical PSNP1; heterozygosity may be a risk factor for both a PSNP1-like syndrome and Parkinson disease; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level.		VAR_019664
	Natural variant	617	1	V → I. Ref.77		VAR_064624
	Natural variant	618	1	P → L in FTD; most common mutation; reduction in the ability to promote microtubule assembly; accelerates aggregation of tau into filaments. Ref.42 Ref.43 Ref.44 Ref.46 Ref.48		VAR_010348
	Natural variant	618	1	P → S in FTD and CBD; reduction in the ability to promote microtubule assembly. Ref.47 Ref.49 Ref.58 Ref.74		VAR_010349
	Natural variant	620	1	G → V in PSNP1. Ref.75		VAR_037439
	Natural variant	622	1	S → N in FTD; minimal parkinsonism; very early age of onset. Ref.53		VAR_010350
	Natural variant	634	1	K → M in FTD. Ref.76		VAR_037440
	Natural variant	637	1	S → F in PIDB; markedly reduced ability of tau to promote microtubule assembly. Ref.64		VAR_019665
	Natural variant	654	1	V → M in FTD; ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease; accelerates aggregation of tau into filaments. Ref.40 Ref.48		VAR_010351
	Natural variant	659	1	E → V in FTD. Ref.54		VAR_019666
	Natural variant	669	1	S → L in fatal respiratory hypoventilation; unusual apparent autosomal recessive inheritance; reduced binding to microtubules as well as increased fibrillization and aggregation. Ref.70		VAR_019667
	Natural variant	686	1	K → I in PIDB; 90% reduction in the rate of microtubule assembly. Ref.61		VAR_019668
	Natural variant	706	1	G → R in PIDB; in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%. Ref.50 Ref.55		VAR_010352
	Natural variant	723	1	R → W in FTD/Alzheimer disease; accelerates aggregation of tau into filaments; reduces tau phosphorylation in cells compared to both the wild-type and other mutant forms. Ref.43 Ref.46 Ref.48 Ref.62 Ref.68 Ref.71		VAR_010353
Experimental info
	Mutagenesis	515	1	S → E: No association with plasma membrane.
	Mutagenesis	516	1	S → E: No association with plasma membrane.
	Mutagenesis	519	1	S → E: No association with plasma membrane.
	Mutagenesis	531	1	S → A: No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein.
	Mutagenesis	548	1	T → A: 50% Decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
	Mutagenesis	548	1	T → E: No association with plasma membrane.
	Mutagenesis	552	1	S → A: 70% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
	Mutagenesis	552	1	S → E: No association with plasma membrane.
	Mutagenesis	579	1	S → A: 8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.
	Mutagenesis	713	1	S → E: No association with plasma membrane.
	Mutagenesis	721	1	S → E: No association with plasma membrane.
	Mutagenesis	726	1	S → E: No association with plasma membrane.
	Mutagenesis	730	1	S → E: No association with plasma membrane.
	Mutagenesis	739	1	S → E: No association with plasma membrane.
	Sequence conflict	48	1	L → P in AAU45390. Ref.6
	Sequence conflict	414	1	H → L in AAC04277. Ref.5
	Sequence conflict	557	1	K → M in AAS17881. Ref.12
	Sequence conflict	591	1	K → S in AAS17881. Ref.12
	Sequence conflict	617	1	V → Q AA sequence Ref.16
	Sequence conflict	622	1	S → K AA sequence Ref.16

Sequences

	Sequence		Length	Mass (Da)
	Isoform PNS-tau [UniParc]. Last modified May 31, 2011. Version 5. Checksum: D46C66CDBCD196E8	FASTA	758	78,928
	10 20 30 40 50 60 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG 70 80 90 100 110 120 SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG 130 140 150 160 170 180 HVTQEPESGK VVQEGFLREP GPPGLSHQLM SGMPGAPLLP EGPREATRQP SGTGPEDTEG 190 200 210 220 230 240 GRHAPELLKH QLLGDLHQEG PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKASPA 250 260 270 280 290 300 QDGRPPQTAA REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSVG RAKGQDAPLE 310 320 330 340 350 360 FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD LPEPSEKQPA 370 380 390 400 410 420 AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS AKTLKNRPCL SPKHPTPGSS 430 440 450 460 470 480 DPLIQPSSPA VCPEPPSSPK YVSSVTSRTG SSGAKEMKLK GADGKTKIAT PRGAAPPGQK 490 500 510 520 530 540 GQANATRIPA KTPPAPKTPP SSGEPPKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP 550 560 570 580 590 600 KKVAVVRTPP KSPSSAKSRL QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD 610 620 630 640 650 660 LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG GGQVEVKSEK 670 680 690 700 710 720 LDFKDRVQSK IGSLDNITHV PGGGNKKIET HKLTFRENAK AKTDHGAEIV YKSPVVSGDT 730 740 750 SPRHLSNVSS TGSIDMVDSP QLATLADEVS ASLAKQGL
	Isoform Fetal-tau [UniParc]. Checksum: 9B26AEDFF4D2677C	FASTA	352	36,760
	10 20 30 40 50 60 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA 70 80 90 100 110 120 AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA 130 140 150 160 170 180 PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS 190 200 210 220 230 240 AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQIV YKPVDLSKVT SKCGSLGNIH 250 260 270 280 290 300 HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG 310 320 330 340 350 AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL
	Isoform Tau-A [UniParc]. Checksum: 4C86C95F53015575	FASTA	316	32,944
	10 20 30 40 50 60 MLRALQQRKR EAGIGDTPSL EDEAAGHVTQ ARMVSKSKDG TGSDDKKAKG ADGKTKIATP 70 80 90 100 110 120 RGAAPPGQKG QANATRIPAK TPPAPKTPPS SGEPPKSGDR SGYSSPGSPG TPGSRSRTPS 130 140 150 160 170 180 LPTPPTREPK KVAVVRTPPK SPSSAKSRLQ TAPVPMPDLK NVKSKIGSTE NLKHQPGGGK 190 200 210 220 230 240 VQIVYKPVDL SKVTSKCGSL GNIHHKPGGG QVEVKSEKLD FKDRVQSKIG SLDNITHVPG 250 260 270 280 290 300 GGNKKIETHK LTFRENAKAK TDHGAEIVYK SPVVSGDTSP RHLSNVSSTG SIDMVDSPQL 310 ATLADEVSAS LAKQGL
	Isoform Tau-B [UniParc]. Checksum: EA206819FE73B67A	FASTA	381	39,720
	10 20 30 40 50 60 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG 70 80 90 100 110 120 SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT 130 140 150 160 170 180 KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR 190 200 210 220 230 240 SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ 250 260 270 280 290 300 PGGGKVQIVY KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI 310 320 330 340 350 360 THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV 370 380 DSPQLATLAD EVSASLAKQG L
	Isoform Tau-C (Tau-3) [UniParc]. Checksum: A76B304E99E6A978	FASTA	410	42,603
	10 20 30 40 50 60 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG 70 80 90 100 110 120 SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG 130 140 150 160 170 180 HVTQARMVSK SKDGTGSDDK KAKGADGKTK IATPRGAAPP GQKGQANATR IPAKTPPAPK 190 200 210 220 230 240 TPPSSGEPPK SGDRSGYSSP GSPGTPGSRS RTPSLPTPPT REPKKVAVVR TPPKSPSSAK 250 260 270 280 290 300 SRLQTAPVPM PDLKNVKSKI GSTENLKHQP GGGKVQIVYK PVDLSKVTSK CGSLGNIHHK 310 320 330 340 350 360 PGGGQVEVKS EKLDFKDRVQ SKIGSLDNIT HVPGGGNKKI ETHKLTFREN AKAKTDHGAE 370 380 390 400 410 IVYKSPVVSG DTSPRHLSNV SSTGSIDMVD SPQLATLADE VSASLAKQGL
	Isoform Tau-D [UniParc]. Checksum: F3256B0AB87B348D	FASTA	383	40,007
	10 20 30 40 50 60 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA 70 80 90 100 110 120 AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA 130 140 150 160 170 180 PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS 190 200 210 220 230 240 AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK 250 260 270 280 290 300 HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD 310 320 330 340 350 360 NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID 370 380 MVDSPQLATL ADEVSASLAK QGL
	Isoform Tau-E [UniParc]. Checksum: 0D4EABCA15179E7D	FASTA	412	42,967
	10 20 30 40 50 60 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG 70 80 90 100 110 120 SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT 130 140 150 160 170 180 KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR 190 200 210 220 230 240 SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ 250 260 270 280 290 300 PGGGKVQIIN KKLDLSNVQS KCGSKDNIKH VPGGGSVQIV YKPVDLSKVT SKCGSLGNIH 310 320 330 340 350 360 HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG 370 380 390 400 410 AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL
	Isoform Tau-F (Tau-4) [UniParc]. Checksum: 835A8706D847A8CC	FASTA	441	45,850
	10 20 30 40 50 60 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG 70 80 90 100 110 120 SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG 130 140 150 160 170 180 HVTQARMVSK SKDGTGSDDK KAKGADGKTK IATPRGAAPP GQKGQANATR IPAKTPPAPK 190 200 210 220 230 240 TPPSSGEPPK SGDRSGYSSP GSPGTPGSRS RTPSLPTPPT REPKKVAVVR TPPKSPSSAK 250 260 270 280 290 300 SRLQTAPVPM PDLKNVKSKI GSTENLKHQP GGGKVQIINK KLDLSNVQSK CGSKDNIKHV 310 320 330 340 350 360 PGGGSVQIVY KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI 370 380 390 400 410 420 THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV 430 440 DSPQLATLAD EVSASLAKQG L
	Isoform Tau-G [UniParc]. Checksum: 13E913ACD1790C26	FASTA	776	80,941
	10 20 30 40 50 60 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG 70 80 90 100 110 120 SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG 130 140 150 160 170 180 HVTQEPESGK VVQEGFLREP GPPGLSHQLM SGMPGAPLLP EGPREATRQP SGTGPEDTEG 190 200 210 220 230 240 GRHAPELLKH QLLGDLHQEG PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKASPA 250 260 270 280 290 300 QDGRPPQTAA REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSVG RAKGQDAPLE 310 320 330 340 350 360 FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD LPEPSEKQPA 370 380 390 400 410 420 AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS AKTLKNRPCL SPKHPTPGSS 430 440 450 460 470 480 DPLIQPSSPA VCPEPPSSPK YVSSVTSRTG SSGAKEMKLK GADGKTKIAT PRGAAPPGQK 490 500 510 520 530 540 GQANATRIPA KTPPAPKTPP SSATKQVQRR PPPAGPRSER GEPPKSGDRS GYSSPGSPGT 550 560 570 580 590 600 PGSRSRTPSL PTPPTREPKK VAVVRTPPKS PSSAKSRLQT APVPMPDLKN VKSKIGSTEN 610 620 630 640 650 660 LKHQPGGGKV QIINKKLDLS NVQSKCGSKD NIKHVPGGGS VQIVYKPVDL SKVTSKCGSL 670 680 690 700 710 720 GNIHHKPGGG QVEVKSEKLD FKDRVQSKIG SLDNITHVPG GGNKKIETHK LTFRENAKAK 730 740 750 760 770 TDHGAEIVYK SPVVSGDTSP RHLSNVSSTG SIDMVDSPQL ATLADEVSAS LAKQGL

References

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[1]	"Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau." Goedert M., Wischik C., Crowther R., Walker J., Klug A. Proc. Natl. Acad. Sci. U.S.A. 85:4051-4055(1988) [PubMed: 3131773] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FETAL-TAU). Tissue: Brain.
[2]	"Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain." Goedert M., Spillantini M.G., Potier M.-C., Ulrich J., Crowther R.A. EMBO J. 8:393-399(1989) [PubMed: 2498079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-D). Tissue: Brain.
[3]	"The microtubule binding domain of tau protein." Lee G., Neve R.L., Kosik K.S. Neuron 2:1615-1624(1989) [PubMed: 2516729] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A AND FETAL-TAU). Tissue: Fetal brain.
[4]	"Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease." Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A. Neuron 3:519-526(1989) [PubMed: 2484340] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-B; TAU-C; TAU-E AND TAU-F). Tissue: Brain.
[5]	"Structure and novel exons of the human tau gene." Andreadis A., Brown W.M., Kosik K.S. Biochemistry 31:10626-10633(1992) [PubMed: 1420178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS PNS-TAU; FETAL-TAU AND TAU-F), ALTERNATIVE SPLICING, VARIANT HIS-441.
[6]	"Cloning of tau-related genes." Chun J., Kwon T., Lee E.-J., Hyun S.-H., Kang S.S. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAU-E).
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FETAL-TAU).
[8]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FETAL-TAU AND TAU-D). Tissue: Brain.
[10]	"Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain." Hasegawa M., Morishima-Kawashima M., Takio K., Suzuki M., Titani K., Ihara Y. J. Biol. Chem. 267:17047-17054(1992) [PubMed: 1512244] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-73; 103-381; 468-497; 508-571; 577-583; 592-607; 616-634; 639-657; 661-664; 671-700 AND 703-758. Tissue: Brain.
[11]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 25-44; 529-538; 560-571 AND 671-686, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[12]	"Molecular interactions of recombinant neural protein tau with recombinant and native PrP proteins in vitro." Han J., Zhang J., Dong X.-P. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 466-740 (ISOFORMS TAU-A/TAU-B/TAU-C/FETAL-TAU).
[13]	"Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation." Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J. J. Biol. Chem. 281:10825-10838(2006) [PubMed: 16443603] [Abstract] Cited for: PROTEIN SEQUENCE OF 543-551; 560-574; 576-584 AND 623-634, PHOSPHORYLATION AT SER-531; THR-534; THR-548; SER-552; SER-554; SER-579; SER-713 AND SER-739, UBIQUITINATION AT LYS-571; LYS-628 AND LYS-670, MASS SPECTROMETRY.
[14]	"Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262." Drewes G., Trinczek B., Illenberger S., Biernat J., Schmitt-Ulms G., Meyer H.E., Mandelkow E.-M., Mandelkow E. J. Biol. Chem. 270:7679-7688(1995) [PubMed: 7706316] [Abstract] Cited for: PROTEIN SEQUENCE OF 577-584; 608-611; 616-628; 639-648 AND 671-686, PHOSPHORYLATION, MUTAGENESIS.
[15]	"A distinct form of tau is selectively incorporated into Alzheimer's paired helical filaments." Mori H., Hamada Y., Kawaguchi M., Honda T., Kondo J., Ihara Y. Biochem. Biophys. Res. Commun. 159:1221-1226(1989) [PubMed: 2495000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 592-622 (ISOFORMS PNS-TAU/TAU-D/TAU-E/TAU-F). Tissue: Brain.
[16]	"Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer's disease." Jakes R., Novak M., Davison M., Wischik C.M. EMBO J. 10:2725-2729(1991) [PubMed: 1915258] [Abstract] Cited for: PROTEIN SEQUENCE OF 616-712.
[17]	"The role of tau (MAPT) in frontotemporal dementia and related tauopathies." Rademakers R., Cruts M., van Broeckhoven C. Hum. Mutat. 24:277-295(2004) [PubMed: 15365985] [Abstract] Cited for: IDENTIFICATION (ISOFORM TAU-G), VARIANT HIS-441.
[18]	"Molecular characterization of microtubule-associated proteins tau and MAP2." Goedert M., Crowther R.A., Garner C.C. Trends Neurosci. 14:193-199(1991) [PubMed: 1713721] [Abstract] Cited for: REVIEW.
[19]	"The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase." Paudel H.K. J. Biol. Chem. 272:1777-1785(1997) [PubMed: 8999860] [Abstract] Cited for: PHOSPHORYLATION AT SER-554; SER-579; SER-602; SER-606 AND SER-669.
[20]	"Characterization of in vitro glycation sites of tau." Nacharaju P., Ko L., Yen S.H. J. Neurochem. 69:1709-1719(1997) [PubMed: 9326300] [Abstract] Cited for: GLYCATION AT LYS-87; LYS-383; LYS-467; LYS-480; LYS-491; LYS-542; LYS-551; LYS-576; LYS-597; LYS-598; LYS-664; LYS-670 AND LYS-686, LACK OF GLYCATION AT LYS-24; LYS-44; LYS-67; LYS-381; LYS-391; LYS-392; LYS-394; LYS-465; LYS-497; LYS-507; LYS-541; LYS-557; LYS-571; LYS-574; LYS-584; LYS-591; LYS-607; LYS-611; LYS-615; LYS-628; LYS-634; LYS-638; LYS-648; LYS-657; LYS-660; LYS-687; LYS-692; LYS-700; LYS-702; LYS-712 AND LYS-755.
[21]	"Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules." Sengupta A., Kabat J., Novak M., Wu Q., Grundke-Iqbal I., Iqbal K. Arch. Biochem. Biophys. 357:299-309(1998) [PubMed: 9735171] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS.
[22]	"The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease." Illenberger S., Zheng-Fischhofer Q., Preuss U., Stamer K., Baumann K., Trinczek B., Biernat J., Godemann R., Mandelkow E.-M., Mandelkow E. Mol. Biol. Cell 9:1495-1512(1998) [PubMed: 9614189] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS.
[23]	"Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments." Maas T., Eidenmueller J., Brandt R. J. Biol. Chem. 275:15733-15740(2000) [PubMed: 10747907] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[24]	"Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules." Li G., Yin H., Kuret J. J. Biol. Chem. 279:15938-15945(2004) [PubMed: 14761950] [Abstract] Cited for: PHOSPHORYLATION AT SER-519; THR-522; SER-713 AND SER-721 BY CSNK1D/CK1, INTERACTION WITH CSNK1D.
[25]	"Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules." Cho J.H., Johnson G.V. J. Neurochem. 88:349-358(2004) [PubMed: 14690523] [Abstract] Cited for: PHOSPHORYLATION AT THR-548 BY GSK3B.
[26]	"Phosphorylation of tau by fyn: implications for Alzheimer's disease." Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K., Fang S.M., Do L.H., Andreadis A., Van Hoesen G., Ksiezak-Reding H. J. Neurosci. 24:2304-2312(2004) [PubMed: 14999081] [Abstract] Cited for: PHOSPHORYLATION AT TYR-18 BY FYN.
[27]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation." Babu J.R., Geetha T., Wooten M.W. J. Neurochem. 94:192-203(2005) [PubMed: 15953362] [Abstract] Cited for: INTERACTION WITH SQSTM1, UBIQUITINATION, PROTEASOMAL DEGRADATION.
[29]	"Phosphoproteomic analysis of synaptosomes from human cerebral cortex." DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A. J. Proteome Res. 4:306-315(2005) [PubMed: 15822905] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; THR-548; SER-673; SER-713; THR-720 AND SER-721, MASS SPECTROMETRY. Tissue: Brain cortex.
[30]	"Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation." Sato S., Cerny R.L., Buescher J.L., Ikezu T. J. Neurochem. 98:1573-1584(2006) [PubMed: 16923168] [Abstract] Cited for: PHOSPHORYLATION AT TYR-514; SER-515; SER-516; SER-519; SER-733; SER-739 AND THR-744.
[31]	"Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite formation through microtubule depolymerization by SGK1 and by SGK1 phosphorylation of tau." Yang Y.C., Lin C.H., Lee E.H. Mol. Cell. Biol. 26:8357-8370(2006) [PubMed: 16982696] [Abstract] Cited for: PHOSPHORYLATION AT SER-214 BY SGK1, INTERACTION WITH SGK1.
[32]	"Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis." Hanger D.P., Byers H.L., Wray S., Leung K.-Y., Saxton M.J., Seereeram A., Reynolds C.H., Ward M.A., Anderton B.H. J. Biol. Chem. 282:23645-23654(2007) [PubMed: 17562708] [Abstract] Cited for: PHOSPHORYLATION BY CSNK1D/CK1.
[33]	"Role for DYRK family kinases on regulation of apoptosis." Yoshida K. Biochem. Pharmacol. 76:1389-1394(2008) [PubMed: 18599021] [Abstract] Cited for: PHOSPHORYLATION AT THR-529 BY DYRK2.
[34]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-548 AND SER-552, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[35]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; THR-529; THR-534 AND SER-721, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516; SER-519; THR-522; SER-579; SER-717 AND SER-721, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[37]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519; SER-713; SER-717; SER-721 AND SER-726, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[38]	"1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides." Wintjens R., Wieruszeski J.-M., Drobecq H., Rousselot-Pailley P., Buee L., Lippens G., Landrieu I. J. Biol. Chem. 276:25150-25156(2001) [PubMed: 11313338] [Abstract] Cited for: STRUCTURE BY NMR OF 542-554 IN COMPLEX WITH PIN1.
[39]	"Tau mutations in frontotemporal dementia FTDP-17 and their relevance for Alzheimer's disease." Goedert M., Spillantini M.G. Biochim. Biophys. Acta 1502:110-121(2000) [PubMed: 10899436] [Abstract] Cited for: REVIEW ON VARIANTS.
[40]	"Tau is a candidate gene for chromosome 17 frontotemporal dementia." Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., Anderson L., Andreadis A., Wiederholt W.C., Raskind M., Schellenberg G.D. Ann. Neurol. 43:815-825(1998) [PubMed: 9629852] [Abstract] Cited for: VARIANT FTD MET-654, VARIANTS ASN-285; ALA-289; HIS-441 AND PRO-447.
[41]	Erratum Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., Anderson L., Andreadis A., Wiederholt W.C., Raskind M., Schellenberg G.D. Ann. Neurol. 44:428-428(1998)
[42]	"Segregation of a missense mutation in the microtubule-associated protein tau gene with familial frontotemporal dementia and parkinsonism." Dumanchin C., Camuzat A., Campion D., Verpillat P., Hannequin D., Dubois B., Saugier-Veber P., Martin C., Penet C., Charbonnier F., Agid Y., Frebourg T., Brice A. Hum. Mol. Genet. 7:1825-1829(1998) [PubMed: 9736786] [Abstract] Cited for: VARIANT FTD LEU-618.
[43]	"Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17." Hutton M., Lendon C.L., Rizzu P., Baker M., Froelich S., Houlden H., Pickering-Brown S., Chakraverty S., Isaacs A., Grover A., Hackett J., Adamson J., Lincoln S., Dickson D., Davies P., Petersen R.C., Stevens M., de Graaff E. , Wauters E., van Baren J., Hillebrand M., Joosse M., Kwon J.M., Nowotny P., Che L.K., Norton J., Morris J.C., Reed L.A., Trojanowski J., Basun H., Lannfelt L., Neystat M., Fahn S., Dark F., Tannenberg T., Dodd P.R., Hayward N., Kwok J.B.J., Schofield P.R., Andreadis A., Snowden J., Craufurd D., Neary D., Owen F., Oostra B.A., Hardy J., Goate A., van Swieten J., Mann D., Lynch T., Heutink P. Nature 393:702-705(1998) [PubMed: 9641683] [Abstract] Cited for: VARIANTS FTD VAL-589; LEU-618 AND TRP-723.
[44]	"Pathogenic implications of mutations in the tau gene in pallido-ponto-nigral degeneration and related neurodegenerative disorders linked to chromosome 17." Clark L.N., Poorkaj P., Wszolek Z., Geschwind D.H., Nasreddine Z.S., Miller B., Li D., Payami H., Awert F., Markopoulou K., Andreadis A., D'Souza I., Lee V.M.-Y., Reed L., Trojanowski J.Q., Zhukareva V., Bird T., Schellenberg G., Wilhelmsen K.C. Proc. Natl. Acad. Sci. U.S.A. 95:13103-13107(1998) [PubMed: 9789048] [Abstract] Cited for: VARIANTS FTD LYS-596 AND LEU-618.
[45]	"A mutation at codon 279 (N279K) in exon 10 of the Tau gene causes a tauopathy with dementia and supranuclear palsy." Delisle M.-B., Murrell J.R., Richardson R., Trofatter J.A., Rascol O., Soulages X., Mohr M., Calvas P., Ghetti B. Acta Neuropathol. 98:62-77(1999) [PubMed: 10412802] [Abstract] Cited for: VARIANT PPND LYS-596.
[46]	"High prevalence of mutations in the microtubule-associated protein tau in a population study of frontotemporal dementia in the Netherlands." Rizzu P., Van Swieten J.C., Joosse M., Hasegawa M., Stevens M., Tibben A., Niermeijer M.F., Hillebrand M., Ravid R., Oostra B.A., Goedert M., van Duijn C.M., Heutink P. Am. J. Hum. Genet. 64:414-421(1999) [PubMed: 9973279] [Abstract] Cited for: VARIANTS FTD VAL-589; LYS-597 DEL; LEU-618 AND TRP-723.
[47]	"FTDP-17: an early-onset phenotype with parkinsonism and epileptic seizures caused by a novel mutation." Sperfeld A.D., Collatz M.B., Baier H., Palmbach M., Storch A., Schwarz J., Tatsch K., Reske S., Joosse M., Heutink P., Ludolph A.C. Ann. Neurol. 46:708-715(1999) [PubMed: 10553987] [Abstract] Cited for: VARIANT FTD SER-618.
[48]	"Accelerated filament formation from tau protein with specific FTDP-17 missense mutations." Nacharaju P., Lewis J., Easson C., Yen S., Hackett J., Hutton M., Yen S.H. FEBS Lett. 447:195-199(1999) [PubMed: 10214944] [Abstract] Cited for: VARIANTS FTD LEU-618; MET-654 AND TRP-723.
[49]	"Frontotemporal dementia and corticobasal degeneration in a family with a P301S mutation in tau." Bugiani O., Murrell J.R., Giaccone G., Hasegawa M., Ghigo G., Tabaton M., Morbin M., Primavera A., Carella F., Solaro C., Grisoli M., Savoiardo M., Spillantini M.G., Tagliavini F., Goedert M., Ghetti B. J. Neuropathol. Exp. Neurol. 58:667-677(1999) [PubMed: 10374757] [Abstract] Cited for: VARIANT FTD/CBD SER-618.
[50]	"Tau gene mutation G389R causes a tauopathy with abundant pick body-like inclusions and axonal deposits." Murrell J.R., Spillantini M.G., Zolo P., Guazzelli M., Smith M.J., Hasegawa M., Redi F., Crowther R.A., Pietrini P., Ghetti B., Goedert M. J. Neuropathol. Exp. Neurol. 58:1207-1226(1999) [PubMed: 10604746] [Abstract] Cited for: VARIANT PIDB ARG-706.
[51]	"A mutation in the microtubule-associated protein tau in pallido-nigro-luysian degeneration." Yasuda M., Kawamata T., Komure O., Kuno S., D'Souza I., Poorkaj P., Kawai J., Tanimukai S., Yamamoto Y., Hasegawa H., Sasahara M., Hazama F., Schellenberg G.D., Tanaka C. Neurology 53:864-868(1999) [PubMed: 10489057] [Abstract] Cited for: VARIANT FTD LYS-596.
[52]	"Mutational analysis of the tau gene in progressive supranuclear palsy." Higgins J.J., Adler R.L., Loveless J.M. Neurology 53:1421-1424(1999) [PubMed: 10534245] [Abstract] Cited for: VARIANTS PSNP1 ASN-285 AND ALA-289.
[53]	"A distinct familial presenile dementia with a novel missense mutation in the tau gene." Iijima M., Tabira T., Poorkaj P., Schellenberg G.D., Trojanowski J.Q., Lee V.M.-Y., Schmidt M.L., Takahashi K., Nabika T., Matsumoto T., Yamashita Y., Yoshioka S., Ishino H. NeuroReport 10:497-501(1999) [PubMed: 10208578] [Abstract] Cited for: VARIANT FTD ASN-622.
[54]	"Frontotemporal dementia with novel tau pathology and a Glu342Val tau mutation." Lippa C.F., Zhukareva V., Kawarai T., Uryu K., Shafiq M., Nee L.E., Grafman J., Liang Y., St George-Hyslop P.H., Trojanowski J.Q., Lee V.M.-Y. Ann. Neurol. 48:850-858(2000) [PubMed: 11117541] [Abstract] Cited for: VARIANT FTD VAL-659.
[55]	"Pick's disease is associated with mutations in the tau gene." Pickering-Brown S., Baker M., Yen S.-H., Liu W.-K., Hasegawa M., Cairns N., Lantos P.L., Rossor M., Iwatsubo T., Davies Y., Allsop D., Furlong R., Owen F., Hardy J., Mann D., Hutton M. Ann. Neurol. 48:859-867(2000) [PubMed: 11117542] [Abstract] Cited for: VARIANTS PIDB THR-574 AND ARG-706, CHARACTERIZATION OF VARIANTS PIDB THR-574 AND ARG-706.
[56]	"Tau gene mutation K257T causes a tauopathy similar to Pick's disease." Rizzini C., Goedert M., Hodges J.R., Smith M.J., Jakes R., Hills R., Xuereb J.H., Crowther R.A., Spillantini M.G. J. Neuropathol. Exp. Neurol. 59:990-1001(2000) [PubMed: 11089577] [Abstract] Cited for: VARIANT PIDB THR-574.
[57]	"Two brothers with frontotemporal dementia and parkinsonism with an N279K mutation of the tau gene." Arima K., Kowalska A., Hasegawa M., Mukoyama M., Watanabe R., Kawai M., Takahashi K., Iwatsubo T., Tabira T., Sunohara N. Neurology 54:1787-1795(2000) [PubMed: 10802785] [Abstract] Cited for: VARIANT FTD LYS-596.
[58]	"A Japanese patient with frontotemporal dementia and parkinsonism by a tau P301S mutation." Yasuda M., Yokoyama K., Nakayasu T., Nishimura Y., Matsui M., Yokoyama T., Miyoshi K., Tanaka C. Neurology 55:1224-1227(2000) [PubMed: 11071507] [Abstract] Cited for: VARIANT FTD SER-618.
[59]	"Familial frontotemporal dementia and parkinsonism with a novel N296H mutation in exon 10 of the tau gene and a widespread tau accumulation in the glial cells." Iseki E., Matsumura T., Marui W., Hino H., Odawara T., Sugiyama N., Suzuki K., Sawada H., Arai T., Kosaka K. Acta Neuropathol. 102:285-292(2001) [PubMed: 11585254] [Abstract] Cited for: VARIANT FTD HIS-613.
[60]	"Familial atypical progressive supranuclear palsy associated with homozigosity for the delN296 mutation in the tau gene." Pastor P., Pastor E., Carnero C., Vela R., Garcia T., Amer G., Tolosa E., Oliva R. Ann. Neurol. 49:263-267(2001) [PubMed: 11220749] [Abstract] Cited for: VARIANT PSNP1 ASN-613 DEL.
[61]	"Pick's disease associated with the novel Tau gene mutation K369I." Neumann M., Schulz-Schaeffer W., Crowther R.A., Smith M.J., Spillantini M.G., Goedert M., Kretzschmar H.A. Ann. Neurol. 50:503-513(2001) [PubMed: 11601501] [Abstract] Cited for: VARIANT PIDB ILE-686, CHARACTERIZATION OF VARIANT PIDB ILE-686.
[62]	"Effects of FTDP-17 mutations on the in vitro phosphorylation of tau by glycogen synthase kinase 3beta identified by mass spectrometry demonstrate certain mutations exert long-range conformational changes." Connell J.W., Gibb G.M., Betts J.C., Blackstock W.P., Gallo J.-M., Lovestone S., Hutton M., Anderton B.H. FEBS Lett. 493:40-44(2001) [PubMed: 11278002] [Abstract] Cited for: CHARACTERIZATION OF VARIANT FTD TRP-723.
[63]	"Clinical and genetic studies of families with the tau N279K mutation (FTDP-17)." Tsuboi Y., Baker M., Hutton M.L., Uitti R.J., Rascol O., Delisle M.-B., Soulages X., Murrell J.R., Ghetti B., Yasuda M., Komure O., Kuno S., Arima K., Sunohara N., Kobayashi T., Mizuno Y., Wszolek Z.K. Neurology 59:1791-1793(2002) [PubMed: 12473774] [Abstract] Cited for: VARIANT FTD LYS-596.
[64]	"A novel tau mutation, S320F, causes a tauopathy with inclusions similar to those in Pick's disease." Rosso S.M., Van Herpen E., Deelen W., Kamphorst W., Severijnen L.-A., Willemsen R., Ravid R., Niermeijer M.F., Dooijes D., Smith M.J., Goedert M., Heutink P., Van Swieten J.C. Ann. Neurol. 51:373-376(2002) [PubMed: 11891833] [Abstract] Cited for: VARIANT PIDB PHE-637, CHARACTERIZATION OF VARIANT PIDB PHE-637.
[65]	"Late-onset frontotemporal dementia with a novel exon 1 (Arg5His) tau gene mutation." Hayashi S., Toyoshima Y., Hasegawa M., Umeda Y., Wakabayashi K., Tokiguchi S., Iwatsubo T., Takahashi H. Ann. Neurol. 51:525-530(2002) [PubMed: 11921059] [Abstract] Cited for: VARIANT FTD HIS-5, CHARACTERIZATION OF VARIANT FTD HIS-5.
[66]	"An R5L tau mutation in a subject with a progressive supranuclear palsy phenotype." Poorkaj P., Muma N.A., Zhukareva V., Cochran E.J., Shannon K.M., Hurtig H., Koller W.C., Bird T.D., Trojanowski J.Q., Lee V.M.-Y., Schellenberg G.D. Ann. Neurol. 52:511-516(2002) [PubMed: 12325083] [Abstract] Cited for: VARIANT PSNP1 LEU-5, CHARACTERIZATION OF VARIANT PSNP1 LEU-5.
[67]	"Functional effects of tau gene mutations deltaN296 and N296H." Yoshida H., Crowther R.A., Goedert M. J. Neurochem. 80:548-551(2002) [PubMed: 11906000] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS FTD ASN-613 DEL AND HIS-613.
[68]	"Early-onset, rapidly progressive familial tauopathy with R406W mutation." Saito Y., Geyer A., Sasaki R., Kuzuhara S., Nanba E., Miyasaka T., Suzuki K., Murayama S. Neurology 58:811-813(2002) [PubMed: 11889249] [Abstract] Cited for: VARIANT FTD TRP-723.
[69]	"A novel L266V mutation of the tau gene causes frontotemporal dementia with a unique tau pathology." Kobayashi T., Ota S., Tanaka K., Ito Y., Hasegawa M., Umeda Y., Motoi Y., Takanashi M., Yasuhara M., Anno M., Mizuno Y., Mori H. Ann. Neurol. 53:133-137(2003) [PubMed: 12509859] [Abstract] Cited for: VARIANT FTD VAL-583, CHARACTERIZATION OF VARIANT FTD VAL-583.
[70]	"An English kindred with a novel recessive tauopathy and respiratory failure." Nicholl D.J., Greenstone M.A., Clarke C.E., Rizzu P., Crooks D., Crowe A., Trojanowski J.Q., Lee V.M.-Y., Heutink P. Ann. Neurol. 54:682-686(2003) [PubMed: 14595660] [Abstract] Cited for: VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669, CHARACTERIZATION OF VARIANT FATAL RESPIRATORY HYPOVENTILATION LEU-669.
[71]	"Tau (MAPT) mutation arg406trp presenting clinically with Alzheimer disease does not share a common founder in western Europe." Rademakers R., Dermaut B., Peeters K., Cruts M., Heutink P., Goate A., Van Broeckhoven C. Hum. Mutat. 22:409-411(2003) [PubMed: 14517953] [Abstract] Cited for: VARIANT FTDP17/ALZHEIMER DISEASE TRP-723.
[72]	"Progressive supranuclear palsy and Parkinson's disease in a family with a new mutation in the tau gene." Rossi G., Gasparoli E., Pasquali C., Di Fede G., Testa D., Albanese A., Bracco F., Tagliavini F. Ann. Neurol. 55:448-448(2004) [PubMed: 14991829] [Abstract] Cited for: VARIANT ATYPICAL PSNP1 ASN-613 DEL.
[73]	"Tau gene delN296 mutation, Parkinson's disease, and atypical supranuclear palsy." Oliva R., Pastor P. Ann. Neurol. 55:448-449(2004) [PubMed: 14991828] [Abstract] Cited for: VARIANT PSNP1/ATYPICAL PSNP1 ASN-613 DEL.
[74]	"Phenotypic heterogeneity within a new family with the MAPT P301S mutation." Yasuda M., Nakamura Y., Kawamata T., Kaneyuki H., Maeda K., Komure O. Ann. Neurol. 58:920-928(2005) [PubMed: 16240366] [Abstract] Cited for: VARIANT FTD SER-618.
[75]	"A new mutation of the tau gene, G303V, in early-onset familial progressive supranuclear palsy." Ros R., Thobois S., Streichenberger N., Kopp N., Sanchez M.P., Perez M., Hoenicka J., Avila J., Honnorat J., de Yebenes J.G. Arch. Neurol. 62:1444-1450(2005) [PubMed: 16157753] [Abstract] Cited for: VARIANT PSNP1 VAL-620.
[76]	"A novel mutation (K317M) in the MAPT gene causes FTDP and motor neuron disease." Zarranz J.J., Ferrer I., Lezcano E., Forcadas M.I., Eizaguirre B., Atares B., Puig B., Gomez-Esteban J.C., Fernandez-Maiztegui C., Rouco I., Perez-Concha T., Fernandez M., Rodriguez O., Rodriguez-Martinez A.B., de Pancorbo M.M., Pastor P., Perez-Tur J. Neurology 64:1578-1585(2005) [PubMed: 15883319] [Abstract] Cited for: VARIANT FTD MET-634.
[77]	"A thorough assessment of benign genetic variability in GRN and MAPT." Guerreiro R.J., Washecka N., Hardy J., Singleton A. Hum. Mutat. 31:E1126-E1140(2010) [PubMed: 20020531] [Abstract] Cited for: VARIANTS MET-17; ALA-30 AND ILE-617.
+	Additional computationally mapped references.

Web resources

Alzheimer Research Forum

Tau mutations

Protein Spotlight

Vita minima - Issue 68 of March 2006

GeneReviews

Wikipedia

Tau protein entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03778 mRNA. Translation: AAA60615.1.
X14474 mRNA. Translation: CAA32636.1.
AF047863 , AF027491, AF047856, AF047857, AF027492, AF047858, AF027493, AF047859, AF047860, AF047862, AF027494, AF027495, AF027496 Genomic DNA. Translation: AAC04277.1.
AF027491 , AF027492, AF027493, AF047860, AF047862, AF027495, AF027496, AF047863 Genomic DNA. Translation: AAC04278.1.
AF027491 , AF047856, AF047857, AF027492, AF027493, AF047860, AF047862, AF027494, AF027495, AF027496, AF047863 Genomic DNA. Translation: AAC04279.1.
AF047861 Genomic DNA. No translation available.
AY730549 mRNA. Translation: AAU45390.1.
BT006772 mRNA. Translation: AAP35418.1.
AC004139 Genomic DNA. No translation available.
AC010792 Genomic DNA. No translation available.
AC217771 Genomic DNA. No translation available.
AC217779 Genomic DNA. No translation available.
BC000558 mRNA. Translation: AAH00558.1.
BC098281 mRNA. Translation: AAH98281.1.
BC099721 mRNA. Translation: AAH99721.1.
BC101936 mRNA. Translation: AAI01937.1.
BC114504 mRNA. Translation: AAI14505.1.
BC114948 mRNA. Translation: AAI14949.1.
AY526356 mRNA. Translation: AAS17881.1.
M25298 mRNA. Translation: AAA57264.1.
BN000503 mRNA. Translation: CAG26750.1.

IPI

IPI00025499.
IPI00026836.
IPI00217976.
IPI00220171.
IPI00220173.
IPI00220174.
IPI00220175.
IPI00293683.
IPI00964662.

PIR

I52232.
QRHUT1. JS0370.
QRHUT2. PN0001.
S26663.

RefSeq

NP_001116538.2. NM_001123066.3.
NP_001116539.1. NM_001123067.3.
NP_001190181.1. NM_001203252.1.
NP_005901.2. NM_005910.5.
NP_058518.1. NM_016834.4.
NP_058519.3. NM_016835.4.
NP_058525.1. NM_016841.4.

UniGene

Hs.101174.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I8H	NMR	-	A	542-554	[»]
3FQP	X-ray	1.51	A	623-628	[»]
3OVL	X-ray	1.81	A	623-628	[»]

DisProt

DP00126.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29753N.

IntAct

P10636. 7 interactions.

MINT

MINT-134394.

STRING

P10636.

PTM databases

PhosphoSite

P10636.

Polymorphism databases

DMDM

13124806.

Proteomic databases

PRIDE

P10636.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262410; ENSP00000262410; ENSG00000186868.

GeneID

4137.

KEGG

hsa:4137.

UCSC

uc002ijr.2. human.
uc002ijs.2. human.
uc002ijt.2. human.
uc002iju.2. human.
uc002ijv.2. human.
uc002ijx.2. human.
uc010dau.1. human.

Organism-specific databases

CTD

4137.

GeneCards

GC17P043982.

HGNC

HGNC:6893. MAPT.

HPA

CAB000151.

MIM

157140. gene+phenotype.
172700. phenotype.
260540. phenotype.
600274. phenotype.
601104. phenotype.

neXtProt

NX_P10636.

Orphanet

33540. Familial Parkinson's disease dementia.
282. Frontotemporal dementia.
36385. Frontotemporal dementia and parkinsonism linked to chromosome 17.
2883. Pick disease of brain.
683. Progressive supranuclear palsy.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09726.

GeneTree

ENSGT00530000063491.

HOVERGEN

HBG000991.

OrthoDB

EOG4B8JDC.

Enzyme and pathway databases

Pathway_Interaction_DB

lysophospholipid_pathway. LPA receptor mediated events.
reelinpathway. Reelin signaling pathway.
p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P10636.

Bgee

P10636.

Genevestigator

P10636.

GermOnline

ENSG00000186868. Homo sapiens.

Family and domain databases

InterPro

IPR002955. Tau_protein.
IPR001084. Tau_tubulin-bd.
[Graphical view]

KO

K04380.

Pfam

PF00418. Tubulin-binding. 4 hits.
[Graphical view]

PRINTS

PR01261. TAUPROTEIN.

PROSITE

PS00229. TAU_MAP_1. 4 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

16246.

PMAP-CutDB

P10636.

SOURCE

Search...

Entry information

Entry name

TAU_HUMAN

Accession

Primary (citable) accession number: P10636
Secondary accession number(s): P18518 , Q14799, Q15549, Q15550, Q15551, Q1RMF6, Q53YB1, Q5CZI7, Q5XWF0, Q6QT54, Q9UDJ3, Q9UMH0, Q9UQ96

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	May 31, 2011
Last modified:	January 25, 2012
This is version 176 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.