HUMAN:TAU

From GONUTS

Jump to: navigation, search

Species (Taxon ID)	Homo sapiens (Human). (taxon:9606)
Gene Name(s)	MAPT ( synonyms: MAPTL, MTBT1, TAU )
Protein Name(s)	Microtubule-associated protein tau Neurofibrillary tangle protein Paired helical filament-tau PHF-tau
External Links
UniProt Identifier	TAU_HUMAN
UniProt Accessions	P10636, P18518, Q14799, Q15549, Q15550, Q15551, Q1RMF6, Q53YB1, Q5CZI7, Q5XWF0, Q6QT54, Q9UDJ3, Q9UMH0, Q9UQ96,
EMBL	J03778, X14474, AF047863, AF027491, AF047856, AF047857, AF027492, AF047858, AF027493, AF047859, AF047860, AF047862, AF027494, AF027495, AF027496, AF027491, AF027492, AF027493, AF047860, AF047862, AF027495, AF027496, AF047863, AF027491, AF047856, AF047857, AF027492, AF027493, AF047860, AF047862, AF027494, AF027495, AF027496, AF047863, AF047861, AY730549, BT006772, AC004139, AC010792, AC217771, AC217779, BC000558, BC098281, BC099721, BC101936, BC114504, BC114948, AY526356, M25298, BN000503,
PIR	I52232, JS0370, PN0001, S26663,
RefSeq	NP_001116538.2, NP_001116539.1, NP_001190181.1, NP_005901.2, NP_058518.1, NP_058519.3, NP_058525.1,
PDB	1I8H, 3FQP,
IntAct	P10636,
Ensembl	ENST00000262410,
Pfam	PF00418,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0030424	axon		IDA: Inferred from Direct Assay		C	Source: UniProtKB
	GO:0005829	cytosol		EXP: Inferred from Experiment		C	Source: Reactome
	GO:0030426	growth cone		IDA: Inferred from Direct Assay		C	Source: UniProtKB
	GO:0005874	microtubule	PMCID: PMC2872491	IEA: Inferred from Electronic Annotation	UniProtKB:P10636	C	Figure 2. Phosphorylation induces self-assembly of Tau. Tau self-assembles mainly through the microtubule binding domain in Tau proteins.	complete
	GO:0005875	microtubule associated complex		TAS: Traceable Author Statement		C	Source: ProtInc
	GO:0034399	nuclear periphery		IDA: Inferred from Direct Assay		C	Source: UniProtKB
	GO:0005886	plasma membrane		IDA: Inferred from Direct Assay		C	Source: UniProtKB
	GO:0045298	tubulin complex		IDA: Inferred from Direct Assay		C	Source: UniProtKB
	GO:0034187	apolipoprotein E binding		IPI: Inferred from Physical Interaction		F	Source: BHF-UCL
	GO:0019899	enzyme binding		IPI: Inferred from Physical Interaction		F	Source: UniProtKB
	GO:0042802	identical protein binding		IPI: Inferred from Physical Interaction		F	Source: IntAct
	GO:0071813	lipoprotein particle binding		IPI: Inferred from Physical Interaction		F	Source: UniProtKB
	GO:0008017	microtubule binding		IDA: Inferred from Direct Assay		F	Source: UniProtKB
	GO:0005515	protein binding		IPI: Inferred from Physical Interaction		F	Source: IntAct
	GO:0017124	SH3 domain binding		IPI: Inferred from Physical Interaction		F	Source: UniProtKB
	GO:0005200	structural constituent of cytoskeleton		TAS: Traceable Author Statement		F	Source: ProtInc
	GO:0000226	microtubule cytoskeleton organization		IDA: Inferred from Direct Assay		P	Source: UniProtKB
	GO:0007026	negative regulation of microtubule depolyme...		IEA: Inferred from Electronic Annotation		P	Source: InterPro
	GO:0045773	positive regulation of axon extension		IDA: Inferred from Direct Assay		P	Source: UniProtKB
	GO:0031116	positive regulation of microtubule polymeri...		IDA: Inferred from Direct Assay		P	Source: UniProtKB
	GO:0071109	superior temporal gyrus development		IMP: Inferred from Mutant Phenotype		P	Source: BHF-UCL
	GO:0000226	microtubule cytoskeleton organization	PMID:1057175^[1]	IDA: Inferred from Direct Assay		P
	GO:0005200	structural constituent of cytoskeleton	PMID:2498079^[2]	TAS: Traceable Author Statement		F
	GO:0005515	protein binding	PMID:10987820^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P05549	F
	GO:0005515	protein binding	PMID:10987820^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P08047	F
	GO:0005515	protein binding	PMID:15953362^[4]	IPI: Inferred from Physical Interaction	UniProtKB:P37198	F
	GO:0005515	protein binding	PMID:16275660^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UNE7	F
	GO:0005515	protein binding	PMID:16446437^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P05067	F
	GO:0005515	protein binding	PMID:16446437^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P05067	F
	GO:0005515	protein binding	PMID:16446437^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P49840	F
	GO:0005515	protein binding	PMID:3111527^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P04271	F
	GO:0005515	protein binding	PMID:3111527^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P62158	F
	GO:0005515	protein binding	PMID:9689133^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P49768	F
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005829	cytosol	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0091	C
	GO:0005829	cytosol	PMID:10747907^[9]	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_13414	TAS: Traceable Author Statement		C
	GO:0005856	cytoskeleton	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0206	C
	GO:0005856	cytoskeleton	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0090	C
	GO:0005874	microtubule	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0493	C
	GO:0005875	microtubule associated complex	PMID:10747907^[9]	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C
	GO:0005886	plasma membrane	PMID:8522593^[10]	IDA: Inferred from Direct Assay		C
	GO:0006915	apoptosis	Reactome:REACT_578	TAS: Traceable Author Statement		P
	GO:0006921	cellular component disassembly involved in apoptosis	Reactome:REACT_995	TAS: Traceable Author Statement		P
	GO:0007026	negative regulation of microtubule depolymerization	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001084	P
	GO:0008017	microtubule binding	PMID:1918161^[11]	IDA: Inferred from Direct Assay		F
	GO:0008219	cell death	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0523	P
	GO:0010506	regulation of autophagy	PMID:19074461^[12]	IGI: Inferred from Genetic Interaction	UniProtKB:O15118	P
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0017124	SH3 domain binding	PMID:9763511^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P06241	F
	GO:0017124	SH3 domain binding	PMID:9763511^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P12931	F
	GO:0019899	enzyme binding	PMID:12888622^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P29466	F
	GO:0019899	enzyme binding	PMID:12888622^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P55210	F
	GO:0019899	enzyme binding	PMID:12888622^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P55212	F
	GO:0019899	enzyme binding	PMID:12888622^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q14790	F
	GO:0019899	enzyme binding	PMID:20133804^[15]	IPI: Inferred from Physical Interaction	UniProtKB:P27124	F
	GO:0019899	enzyme binding	PMID:9736630^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P42574	F
	GO:0030424	axon	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0279	C
	GO:0030424	axon	PMID:8642405^[17]	IDA: Inferred from Direct Assay		C
	GO:0030426	growth cone	PMID:8642405^[17]	IDA: Inferred from Direct Assay		C
	GO:0031113	regulation of microtubule polymerization	PMID:1057175^[1]	NAS: Non-traceable Author Statement		P
	GO:0031116	positive regulation of microtubule polymerization	PMID:1421571^[18]	IDA: Inferred from Direct Assay		P
	GO:0034187	apolipoprotein E binding	PMID:7566652^[19]	IPI: Inferred from Physical Interaction	UniProtKB:P02649	F
	GO:0034399	nuclear periphery	PMID:19157893^[20]	IDA: Inferred from Direct Assay		C
	GO:0042802	identical protein binding	PMID:16446437^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P10636	F
	GO:0042995	cell projection	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0966	C
	GO:0045298	tubulin complex	PMID:8642405^[17]	IDA: Inferred from Direct Assay		C
	GO:0045773	positive regulation of axon extension	PMID:1389180^[21]	IDA: Inferred from Direct Assay		P
	GO:0048699	generation of neurons	PMID:8522593^[10]	NAS: Non-traceable Author Statement		P
	GO:0071813	lipoprotein particle binding	PMID:7972031^[22]	IPI: Inferred from Physical Interaction	UniProtKB:P02649	F
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Weingarten MD et al. (1975) A protein factor essential for microtubule assembly. Proc Natl Acad Sci U S A 72: 1858-62 PubMed GONUTS page
↑ Goedert M et al. (1989) 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. EMBO J 8: 393-9 PubMed GONUTS page
↑ ^3.0 ^3.1 Heicklen-Klein A & Ginzburg I (2000) Tau promoter confers neuronal specificity and binds Sp1 and AP-2. J Neurochem 75: 1408-18 PubMed GONUTS page
↑ Babu JR et al. (2005) Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation. J Neurochem 94: 192-203 PubMed GONUTS page
↑ Grelle G et al. (2006) Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays. Mol Cell Proteomics 5: 234-44 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Guo JP et al. (2006) Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease. Proc Natl Acad Sci U S A 103: 1953-8 PubMed GONUTS page
↑ ^7.0 ^7.1 Baudier J et al. (1987) Comparison of S100b protein with calmodulin: interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C. Biochemistry 26: 2886-93 PubMed GONUTS page
↑ Takashima A et al. (1998) Presenilin 1 associates with glycogen synthase kinase-3beta and its substrate tau. Proc Natl Acad Sci U S A 95: 9637-41 PubMed GONUTS page
↑ ^9.0 ^9.1 Maas T et al. (2000) Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J Biol Chem 275: 15733-40 PubMed GONUTS page
↑ ^10.0 ^10.1 Brandt R et al. (1995) Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J Cell Biol 131: 1327-40 PubMed GONUTS page
↑ Butner KA & Kirschner MW (1991) Tau protein binds to microtubules through a flexible array of distributed weak sites. J Cell Biol 115: 717-30 PubMed GONUTS page
↑ Pacheco CD et al. (2009) Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis. Hum Mol Genet 18: 956-65 PubMed GONUTS page
↑ ^13.0 ^13.1 Lee G et al. (1998) Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci 111 ( Pt 21): 3167-77 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 Gamblin TC et al. (2003) Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc Natl Acad Sci U S A 100: 10032-7 PubMed GONUTS page
↑ Chambraud B et al. (2010) A role for FKBP52 in Tau protein function. Proc Natl Acad Sci U S A 107: 2658-63 PubMed GONUTS page
↑ Canu N et al. (1998) Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis. J Neurosci 18: 7061-74 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Black MM et al. (1996) Tau is enriched on dynamic microtubules in the distal region of growing axons. J Neurosci 16: 3601-19 PubMed GONUTS page
↑ Drechsel DN et al. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol Biol Cell 3: 1141-54 PubMed GONUTS page
↑ Huang DY et al. (1995) ApoE3 binding to tau tandem repeat I is abolished by tau serine262 phosphorylation. Neurosci Lett 192: 209-12 PubMed GONUTS page
↑ Dinh K et al. (2009) Fluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells. Cytokine 45: 179-83 PubMed GONUTS page
↑ Caceres A et al. (1992) Suppression of MAP2 in cultured cerebellar macroneurons inhibits minor neurite formation. Neuron 9: 607-18 PubMed GONUTS page
↑ Strittmatter WJ et al. (1994) Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: implications for Alzheimer disease. Proc Natl Acad Sci U S A 91: 11183-6 PubMed GONUTS page

[PMID:1057175-0] 1.0 ^1.1 Weingarten MD et al. (1975) A protein factor essential for microtubule assembly. Proc Natl Acad Sci U S A 72: 1858-62 PubMed GONUTS page

[PMID:2498079-1] Goedert M et al. (1989) 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. EMBO J 8: 393-9 PubMed GONUTS page

[PMID:10987820-2] 3.0 ^3.1 Heicklen-Klein A & Ginzburg I (2000) Tau promoter confers neuronal specificity and binds Sp1 and AP-2. J Neurochem 75: 1408-18 PubMed GONUTS page

[PMID:15953362-3] Babu JR et al. (2005) Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation. J Neurochem 94: 192-203 PubMed GONUTS page

[PMID:16275660-4] Grelle G et al. (2006) Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays. Mol Cell Proteomics 5: 234-44 PubMed GONUTS page

[PMID:16446437-5] 6.0 ^6.1 ^6.2 ^6.3 Guo JP et al. (2006) Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease. Proc Natl Acad Sci U S A 103: 1953-8 PubMed GONUTS page

[PMID:3111527-6] 7.0 ^7.1 Baudier J et al. (1987) Comparison of S100b protein with calmodulin: interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C. Biochemistry 26: 2886-93 PubMed GONUTS page

[PMID:9689133-7] Takashima A et al. (1998) Presenilin 1 associates with glycogen synthase kinase-3beta and its substrate tau. Proc Natl Acad Sci U S A 95: 9637-41 PubMed GONUTS page

[PMID:10747907-8] 9.0 ^9.1 Maas T et al. (2000) Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J Biol Chem 275: 15733-40 PubMed GONUTS page

[PMID:8522593-9] 10.0 ^10.1 Brandt R et al. (1995) Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J Cell Biol 131: 1327-40 PubMed GONUTS page

[PMID:1918161-10] Butner KA & Kirschner MW (1991) Tau protein binds to microtubules through a flexible array of distributed weak sites. J Cell Biol 115: 717-30 PubMed GONUTS page

[PMID:19074461-11] Pacheco CD et al. (2009) Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis. Hum Mol Genet 18: 956-65 PubMed GONUTS page

[PMID:9763511-12] 13.0 ^13.1 Lee G et al. (1998) Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci 111 ( Pt 21): 3167-77 PubMed GONUTS page

[PMID:12888622-13] 14.0 ^14.1 ^14.2 ^14.3 Gamblin TC et al. (2003) Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc Natl Acad Sci U S A 100: 10032-7 PubMed GONUTS page

[PMID:20133804-14] Chambraud B et al. (2010) A role for FKBP52 in Tau protein function. Proc Natl Acad Sci U S A 107: 2658-63 PubMed GONUTS page

[PMID:9736630-15] Canu N et al. (1998) Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis. J Neurosci 18: 7061-74 PubMed GONUTS page

[PMID:8642405-16] 17.0 ^17.1 ^17.2 Black MM et al. (1996) Tau is enriched on dynamic microtubules in the distal region of growing axons. J Neurosci 16: 3601-19 PubMed GONUTS page

[PMID:1421571-17] Drechsel DN et al. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol Biol Cell 3: 1141-54 PubMed GONUTS page

[PMID:7566652-18] Huang DY et al. (1995) ApoE3 binding to tau tandem repeat I is abolished by tau serine262 phosphorylation. Neurosci Lett 192: 209-12 PubMed GONUTS page

[PMID:19157893-19] Dinh K et al. (2009) Fluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells. Cytokine 45: 179-83 PubMed GONUTS page

[PMID:1389180-20] Caceres A et al. (1992) Suppression of MAP2 in cultured cerebellar macroneurons inhibits minor neurite formation. Neuron 9: 607-18 PubMed GONUTS page

[PMID:7972031-21] Strittmatter WJ et al. (1994) Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: implications for Alzheimer disease. Proc Natl Acad Sci U S A 91: 11183-6 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

HUMAN:TAU

Contents

Annotations

Notes

References

a

c

e

e cont.

g

h

i

l

m

n

n cont.

p

r

s

t

v

Personal tools

Namespaces

Variants

Views

Actions

Search

Navigation

Cacao

Journal Clubs

page contributors

Toolbox