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Protein

Microtubule-associated protein tau

Gene

MAPT

Organism
Papio hamadryas (Hamadryas baboon)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein tau
Alternative name(s):
Neurofibrillary tangle protein
Paired helical filament-tau
Short name:
PHF-tau
Gene namesi
Name:MAPT
Synonyms:TAU
OrganismiPapio hamadryas (Hamadryas baboon)
Taxonomic identifieri9557 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaePapio

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000727442 – 383Microtubule-associated protein tauAdd BLAST382

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei18PhosphotyrosineBy similarity1
Modified residuei29PhosphotyrosineBy similarity1
Cross-linki44Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei53PhosphothreonineBy similarity1
Modified residuei95PhosphothreonineBy similarity1
Modified residuei97Omega-N-methylarginineBy similarity1
Modified residuei105N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei105N6-acetyllysine; alternateBy similarity1
Modified residuei111PhosphothreonineBy similarity1
Modified residuei117PhosphothreonineBy similarity1
Modified residuei123PhosphothreonineBy similarity1
Modified residuei127PhosphoserineBy similarity1
Modified residuei133PhosphoserineBy similarity1
Modified residuei137PhosphoserineBy similarity1
Modified residuei139PhosphotyrosineBy similarity1
Modified residuei140PhosphoserineBy similarity1
Modified residuei141PhosphoserineBy similarity1
Modified residuei144PhosphoserineBy similarity1
Modified residuei147PhosphothreonineBy similarity1
Modified residuei154PhosphothreonineBy similarity1
Modified residuei156PhosphoserineBy similarity1
Modified residuei159PhosphothreonineBy similarity1
Modified residuei167N6-acetyllysineBy similarity1
Modified residuei173PhosphothreonineBy similarity1
Modified residuei177PhosphoserineBy similarity1
Modified residuei179PhosphoserineBy similarity1
Cross-linki196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei201N6-acetyllysine; alternateBy similarity1
Modified residuei201N6-methyllysine; alternateBy similarity1
Cross-linki201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei204PhosphoserineBy similarity1
Cross-linki209Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei223N6-acetyllysine; alternateBy similarity1
Cross-linki223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei227PhosphoserineBy similarity1
Modified residuei231PhosphoserineBy similarity1
Modified residuei232N6-acetyllysineBy similarity1
Disulfide bondi233 ↔ 264By similarity
Modified residuei235PhosphoserineBy similarity1
Modified residuei240N6-acetyllysine; alternateBy similarity1
Cross-linki240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei247PhosphoserineBy similarity1
Modified residuei253N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei253N6-acetyllysine; alternateBy similarity1
Cross-linki253Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei259N6-acetyllysine; alternateBy similarity1
Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei263N6-acetyllysine; alternateBy similarity1
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei266PhosphoserineBy similarity1
Modified residuei273N6-acetyllysine; alternateBy similarity1
Cross-linki273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei285N6-acetyllysine; alternateBy similarity1
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei289N6-acetyllysine; alternateBy similarity1
Cross-linki289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei291Omega-N-methylarginineBy similarity1
Modified residuei294PhosphoserineBy similarity1
Cross-linki295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei298PhosphoserineBy similarity1
Modified residuei311N6-acetyllysine; alternateBy similarity1
Cross-linki311Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki317Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei327N6-acetyllysine; alternateBy similarity1
Cross-linki327Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei336PhosphotyrosineBy similarity1
Modified residuei338PhosphoserineBy similarity1
Modified residuei342PhosphoserineBy similarity1
Modified residuei345PhosphothreonineBy similarity1
Modified residuei346PhosphoserineBy similarity1
Modified residuei351PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei364PhosphoserineBy similarity1
Modified residuei369PhosphothreonineBy similarity1

Post-translational modificationi

Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity).By similarity
Phosphorylation at various serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5, GSK3, MAPK) (a few sites per protein in interphase, more in mitosis), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1, MARK2, MARK3 or MARK4), causing detachment from microtubules, and their disassembly (By similarity). Phosphorylation at Ser-204 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated by PHK. Dephosphorylation at several serine and threonine residues by the serine/threonine phosphatase PPP5C (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9MYX8

Expressioni

Tissue specificityi

Expressed in neurons.

Interactioni

Subunit structurei

Interacts with MARK1, MARK2, MARK3 AND MARK4 (By similarity). Interacts with SQSTM1 when polyubiquitinated. Interacts with PSMC2 through SQSTM1 (By similarity). Interacts with FKBP4. Binds to CSNK1D (By similarity).By similarity

GO - Molecular functioni

Structurei

3D structure databases

SMRiQ9MYX8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati186 – 216Tau/MAP 1PROSITE-ProRule annotationAdd BLAST31
Repeati217 – 247Tau/MAP 2PROSITE-ProRule annotationAdd BLAST31
Repeati248 – 278Tau/MAP 3PROSITE-ProRule annotationAdd BLAST31
Repeati279 – 310Tau/MAP 4PROSITE-ProRule annotationAdd BLAST32

Domaini

The tau/MAP repeat binds to tubulin.

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG000991

Family and domain databases

InterProiView protein in InterPro
IPR001084 MAP_tubulin-bd_rpt
IPR002955 Tau
PfamiView protein in Pfam
PF00418 Tubulin-binding, 4 hits
PRINTSiPR01261 TAUPROTEIN
PROSITEiView protein in PROSITE
PS00229 TAU_MAP_1, 4 hits
PS51491 TAU_MAP_2, 4 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9MYX8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEPRQEFDV MEDHAGTYGL GDRKDQEGYT MLQDQEGDTD AGLKAEEAGI
60 70 80 90 100
GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA
110 120 130 140 150
PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS
160 170 180 190 200
RSRTPSLPTP PAREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS
210 220 230 240 250
KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI
260 270 280 290 300
VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD
310 320 330 340 350
NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL
360 370 380
SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL
Length:383
Mass (Da):40,011
Last modified:January 23, 2007 - v3
Checksum:iC6184212BB88D29F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF281310 mRNA Translation: AAF97596.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF281310 mRNA Translation: AAF97596.1

3D structure databases

SMRiQ9MYX8
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9MYX8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG000991

Family and domain databases

InterProiView protein in InterPro
IPR001084 MAP_tubulin-bd_rpt
IPR002955 Tau
PfamiView protein in Pfam
PF00418 Tubulin-binding, 4 hits
PRINTSiPR01261 TAUPROTEIN
PROSITEiView protein in PROSITE
PS00229 TAU_MAP_1, 4 hits
PS51491 TAU_MAP_2, 4 hits
ProtoNetiSearch...

Entry informationi

Entry nameiTAU_PAPHA
AccessioniPrimary (citable) accession number: Q9MYX8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 88 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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