P10637

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession TAU_MOUSE; P10637;
Entrez ID 17762
GenBank Protein ID NM_001038609.2; NM_001285454.1; NM_001285455.1; NM_001285456.1; NM_010838.4;
GenBank Nucleotide ID NP_001033698.1; NP_001272383.1; NP_001272384.1; NP_001272385.1; NP_034968.3;
Protein Name Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau)
Gene Name Mapt; Mtapt; Tau
Organism Mus musculus
NCBI Taxa ID 10090
Functional DescriptionPromotes 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.
Sequence
(Fasta)
MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS ETSDAKSTPT 60
AEDVTAPLVD ERAPDKQAAA QPHTEIPEGI TAEEAGIGDT PNQEDQAAGH VTQGRREGQA 120
PDLGTSDWTR QQVSSMSGAP LLPQGLREAT CQPSGTRPED IEKSHPASEL LRRGPPQKEG 180
WGQDRLGSEE EVDEDLTVDE SSQDSPPSQA SLTPGRAAPQ AGSGSVCGET ASVPGLPTEG 240
SVPLPADFFS KVSAETQASQ PEGPGTGPME EGHEAAPEFT FHVEIKASTP KEQDLEGATV 300
VGVPGEEQKA QTQGPSVGKG TKEASLQEPP GKQPAAGLPG RPVSRVPQLK ARVASKDRTG 360
NDEKKAKTST PSCAKAPSHR PCLSPTRPTL GSSDPLIKPS SPAVSPEPAT SPKHVSSVTP 420
RNGSPGTKQM KLKGADGKTG AKIATPRGAA SPAQKGTSNA TRIPAKTTPS PKTPPGSGEP 480
PKSGERSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSA SKSRLQTAPV 540
PMPDLKNVRS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI 600
VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN 660
KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL 720
ADEVSASLAK QGL 734

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Serine PhosphorylationAlzheimer's diseasePS42224660612; 23261664
[Reference]: Most of the human tau-immunoreactive cell groups also showed tau hyperphosphorylation at the epitopes Thr231/Ser235 and Ser202/Thr205, while abnormal tau phosphorylation at the epitope Ser422 or silver stained structures were almost totally lacking.
2Threonine PhosphorylationParkinson's diseaseUT49725394490
[Reference]: GSK-3? dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and ?-synuclein.
3Threonine PhosphorylationParkinson's diseaseUT50425394490
[Reference]: GSK-3? dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and ?-synuclein.
4Serine PhosphorylationAlzheimer's diseaseUS50610460255
[Reference]: cAMP-dependent protein kinase phosphorylations on tau in Alzheimer's disease.
5Serine PhosphorylationParkinson's diseaseUS52725394490
[Reference]: GSK-3? dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and ?-synuclein.
6Serine PhosphorylationParkinson's diseaseUS55425394490
[Reference]: In midbrain, significant hyperphosphorylation in PD mouse model
7Serine PhosphorylationParkinson's diseaseUS64825394490
[Reference]: GSK-3? dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and ?-synuclein.
8Serine PhosphorylationParkinson's diseaseUS68825394490
[Reference]: GSK-3? dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and ?-synuclein.
9Serine PhosphorylationParkinson's diseaseUS70125394490
[Reference]: GSK-3? dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and ?-synuclein.
10Serine PhosphorylationAlzheimer's diseaseUS70110460255
[Reference]: GSK-3? dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and ?-synuclein.
11Serine PhosphorylationParkinson's diseaseUS71425394490
[Reference]: GSK-3? dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and ?-synuclein.

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 19)
(view all)
MESH:D000544 ; Alzheimer Disease
MESH:D003072 ; Cognition Disorders
MESH:D003704 ; Dementia
MESH:D004195 ; Disease Models, Animal
MESH:D057180 ; Frontotemporal Dementia
MESH:D007859 ; Learning Disorders

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 58)
(view all)
100       EEAGIGDTPNQEDQA     dbPAF
188       WGQDRLGSEEEVDED     dbPAF
205       VDESSQDSPPSQASL     dbPAF
208       SSQDSPPSQASLTPG     dbPAF
213       PPSQASLTPGRAAPQ     dbPAF
288       FHVEIKASTPKEQDL     dbPAF
Ubiquitination
(count: 4)
546       PVPMPDLKNVRSKIG     PLMD
573       KVQIINKKLDLSNVQ     PLMD
582       DLSNVQSKCGSKDNI     PLMD
603       GSVQIVYKPVDLSKV     PLMD
Methylation
(count: 1)
551       DLKNVRSKIGSTENL     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource