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Entry version 88 (02 Jun 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Microtubule-associated protein tau

Gene

MAPT

Organism
Spermophilus citellus (European suslik) (Citellus citellus)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.

1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processHibernation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Microtubule-associated protein tau
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MAPT
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSpermophilus citellus (European suslik) (Citellus citellus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9997 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciuromorphaSciuridaeXerinaeMarmotiniSpermophilus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002324542 – 430Microtubule-associated protein tauAdd BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei18PhosphotyrosineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei33PhosphoserineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei56PhosphothreonineBy similarity1
Modified residuei58PhosphothreonineBy similarity1
Modified residuei98PhosphothreonineBy similarity1
Modified residuei142PhosphothreonineBy similarity1
Modified residuei144Omega-N-methylarginineBy similarity1
Modified residuei152N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei152N6-acetyllysine; alternateBy similarity1
Modified residuei158PhosphothreonineBy similarity1
Modified residuei164PhosphothreonineBy similarity1
Modified residuei165PhosphothreonineBy similarity1
Modified residuei170PhosphothreonineBy similarity1
Modified residuei180PhosphoserineBy similarity1
Modified residuei184PhosphoserineBy similarity1
Modified residuei186PhosphotyrosineBy similarity1
Modified residuei187PhosphoserineBy similarity1
Modified residuei188PhosphoserineBy similarity1
Modified residuei191PhosphoserineBy similarity1
Modified residuei194PhosphothreonineBy similarity1
Modified residuei201PhosphothreonineBy similarity1
Modified residuei203PhosphoserineBy similarity1
Modified residuei206PhosphothreonineBy similarity1
Modified residuei214N6-acetyllysineBy similarity1
Modified residuei220PhosphothreonineBy similarity1
Modified residuei224PhosphoserineBy similarity1
Modified residuei226PhosphoserineBy similarity1
Cross-linki243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei248N6-acetyllysine; alternateBy similarity1
Modified residuei248N6-methyllysine; alternateBy similarity1
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei251PhosphoserineBy similarity1
Cross-linki256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei270N6-acetyllysine; alternateBy similarity1
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei274PhosphoserineBy similarity1
Modified residuei278PhosphoserineBy similarity1
Modified residuei279N6-acetyllysineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi280 ↔ 311By similarity
Modified residuei282PhosphoserineBy similarity1
Modified residuei287N6-acetyllysine; alternateBy similarity1
Cross-linki287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei294PhosphoserineBy similarity1
Modified residuei300N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei300N6-acetyllysine; alternateBy similarity1
Cross-linki300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei306N6-acetyllysine; alternateBy similarity1
Cross-linki306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei310N6-acetyllysine; alternateBy similarity1
Cross-linki310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei313PhosphoserineBy similarity1
Modified residuei320N6-acetyllysine; alternateBy similarity1
Cross-linki320Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei332N6-acetyllysine; alternateBy similarity1
Cross-linki332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei336N6-acetyllysine; alternateBy similarity1
Cross-linki336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei338Omega-N-methylarginineBy similarity1
Modified residuei341PhosphoserineBy similarity1
Cross-linki342Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei345PhosphoserineBy similarity1
Modified residuei358N6-acetyllysine; alternateBy similarity1
Cross-linki358Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki364Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei374N6-acetyllysine; alternateBy similarity1
Cross-linki374Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei383PhosphotyrosineBy similarity1
Modified residuei385PhosphoserineBy similarity1
Modified residuei389PhosphoserineBy similarity1
Modified residuei392PhosphothreonineBy similarity1
Modified residuei393PhosphoserineBy similarity1
Modified residuei398PhosphoserineBy similarity1
Modified residuei405PhosphoserineBy similarity1
Modified residuei411PhosphoserineBy similarity1
Modified residuei416PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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-345 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
Hyperphosphorylated (in particular at Thr-170, Ser-191, Thr-194, Ser-251, and Ser-345) during hibernation. Phosphorylation is fully reversible after arousal. Highly phosphorylated tau contains a number of paired helical filaments (PHFs)-like epitopes. PHF-like phosphorylation is not associated with fibril formation. Distribution of PHF-like tau is more intense in the entorhinal cortex, hippocampus and isocortical areas. PHF-like phosphorylation-dephosphorylation during hibernation cycle is synchronized with regression-re-establishment of afferentation. It may reflect a protective mechanism in an unfavorable environment.1 Publication

Keywords - PTMi

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with MARK1, MARK2, MARK3 AND MARK4 (By similarity).

Interacts with SQSTM1 when polyubiquitinated (By similarity).

Interacts with PSMC2 through SQSTM1 (By similarity).

Interacts with FKBP4 (By similarity). Binds to CSNK1D (By similarity).

Interacts with SGK1 (By similarity).

Interacts with PIN1 (By similarity).

Interacts with LRRK2 (By similarity).

Interacts with LRP1, leading to endocytosis; this interaction is reduced in the presence of LRPAP1/RAP (By similarity).

By similarity

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q6TS35

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati233 – 263Tau/MAP 1PROSITE-ProRule annotationAdd BLAST31
Repeati264 – 294Tau/MAP 2PROSITE-ProRule annotationAdd BLAST31
Repeati295 – 325Tau/MAP 3PROSITE-ProRule annotationAdd BLAST31
Repeati326 – 357Tau/MAP 4PROSITE-ProRule annotationAdd BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 245DisorderedSequence analysisAdd BLAST245
Regioni387 – 406DisorderedSequence analysisAdd BLAST20

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 21Basic and acidic residuesSequence analysisAdd BLAST21
Compositional biasi119 – 134Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi149 – 164Polar residuesSequence analysisAdd BLAST16
Compositional biasi184 – 200Polar residuesSequence analysisAdd BLAST17
Compositional biasi391 – 406Polar residuesSequence analysisAdd BLAST16

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The tau/MAP repeat binds to tubulin.By similarity

Keywords - Domaini

Repeat

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001084, MAP_tubulin-bd_rpt
IPR002955, Tau

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00418, Tubulin-binding, 4 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01261, TAUPROTEIN

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00229, TAU_MAP_1, 4 hits
PS51491, TAU_MAP_2, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoform i produced by alternative splicing. AlignAdd to basket
Note: A number of isoforms are produced. 6 isoforms have been detected in the adult brain. The pattern of isoforms and their relative expression levels are unaffected during hibernation cycle.
Isoform 1 (identifier: Q6TS35-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAEPRQEFDT AEDHAEGYAL LQDQEGEHGL KASPLQTPAD DGPEEPVSET
60 70 80 90 100
SDAKSTPTAE DVTAPLVDER TPGEQAATQP PTDIPEGTTA EEAGIGDTPN
110 120 130 140 150
MEDQAAGHVT QARMVSKGKE GTGSEDRKAK GADSKTGTKI ATPRGTAPPG
160 170 180 190 200
QKGTANATRI PAKTTPSPKT PPGTGEPAKS GDRSGYSSPG SPGTPGSRSR
210 220 230 240 250
TPSLPTPPTR EPKKVAVVRT PPKSPSSTKS RLQTAPVPMP DLKNVRSKIG
260 270 280 290 300
STENLKHQPG GGKVQIINKK LDLSNVQSKC GSKDNIKHVP GGGSVQIVYK
310 320 330 340 350
PVDLSKVTSK CGSLGNIHHK PGGGQVEVKS EKLDFKDRVQ SKIGSLDNIT
360 370 380 390 400
HVPGGGNKKI ETHKLTFREN AKAKTDHGAE IVYKSPVVSG DTSPRHLSNV
410 420 430
SSTGSINMVD SPQLATLADE VSASLAKQGL
Length:430
Mass (Da):44,803
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5ED2B0EB0DFADAF0
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY388477 mRNA Translation: AAQ92319.1

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

Vita minima - Issue 68 of March 2006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY388477 mRNA Translation: AAQ92319.1

3D structure databases

SMRiQ6TS35
ModBaseiSearch...

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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTAU_SPECI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6TS35
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 88 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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