CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003820
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-associated protein tau 
Protein Synonyms/Alias
 Neurofibrillary tangle protein; Paired helical filament-tau; PHF-tau 
Gene Name
 MAPT 
Gene Synonyms/Alias
 MAPTL; MTBT1; TAU 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
148KAKGADGKTKIATPRacetylation[1]
150KGADGKTKIATPRGAacetylation[1, 2]
163GAAPPGQKGQANATRacetylation[1, 2]
174NATRIPAKTPPAPKTacetylation[1, 2]
180AKTPPAPKTPPSSGEacetylation[1]
190PSSGEPPKSGDRSGYacetylation[1]
234AVVRTPPKSPSSAKSacetylation[1, 2]
240PKSPSSAKSRLQTAPacetylation[2]
254PVPMPDLKNVKSKIGacetylation[1]
257MPDLKNVKSKIGSTEacetylation[1]
259DLKNVKSKIGSTENLacetylation[1, 2]
267IGSTENLKHQPGGGKacetylation[1]
274KHQPGGGKVQIINKKacetylation[1, 2]
280GKVQIINKKLDLSNVacetylation[1, 2]
281KVQIINKKLDLSNVQacetylation[1, 2]
290DLSNVQSKCGSKDNIacetylation[1, 2]
298CGSKDNIKHVPGGGSacetylation[1]
311GSVQIVYKPVDLSKVacetylation[2]
317YKPVDLSKVTSKCGSacetylation[1]
321DLSKVTSKCGSLGNIacetylation[1]
331SLGNIHHKPGGGQVEacetylation[1]
353FKDRVQSKIGSLDNIacetylation[1]
369HVPGGGNKKIETHKLacetylation[1, 2]
370VPGGGNKKIETHKLTacetylation[1]
383LTFRENAKAKTDHGAacetylation[1]
385FRENAKAKTDHGAEIacetylation[1]
395HGAEIVYKSPVVSGDacetylation[1, 2]
Reference
 [1] Acetylation of tau inhibits its degradation and contributes to tauopathy.
 Min SW, Cho SH, Zhou Y, Schroeder S, Haroutunian V, Seeley WW, Huang EJ, Shen Y, Masliah E, Mukherjee C, Meyers D, Cole PA, Ott M, Gan L.
 Neuron. 2010 Sep 23;67(6):953-66. [PMID: 20869593]
 [2] The acetylation of tau inhibits its function and promotes pathological tau aggregation.
 Cohen TJ, Guo JL, Hurtado DE, Kwong LK, Mills IP, Trojanowski JQ, Lee VM.
 Nat Commun. 2011;2:252. [PMID: 21427723] 
Functional Description
 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/MAPT 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 Annotation
 REPEAT 561 591 Tau/MAP 1.
 REPEAT 592 622 Tau/MAP 2.
 REPEAT 623 653 Tau/MAP 3.
 REPEAT 654 685 Tau/MAP 4.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 46 46 Phosphoserine; by PDPK1.
 MOD_RES 50 50 Phosphothreonine; by PDPK1.
 MOD_RES 111 111 Phosphothreonine (By similarity).
 MOD_RES 214 214 Phosphoserine; by SGK1.
 MOD_RES 470 470 Phosphothreonine; by PDPK1.
 MOD_RES 484 484 Deamidated asparagine; in tau and PHF-
 MOD_RES 492 492 Phosphothreonine; by PDPK1.
 MOD_RES 498 498 Phosphothreonine; by PDPK1.
 MOD_RES 514 514 Phosphotyrosine; by TTBK1.
 MOD_RES 515 515 Phosphoserine; by PDPK1 and TTBK1.
 MOD_RES 516 516 Phosphoserine; by PDPK1 and TTBK1.
 MOD_RES 519 519 Phosphoserine; by CK1, PDPK1 and TTBK1.
 MOD_RES 522 522 Phosphothreonine; by CK1 and PDPK1.
 MOD_RES 529 529 Phosphothreonine; by BRSK1, BRSK2, DYRK2
 MOD_RES 531 531 Phosphoserine; by PKA.
 MOD_RES 534 534 Phosphothreonine; by PDPK1.
 MOD_RES 548 548 Phosphothreonine; by GSK3-beta and PDPK1.
 MOD_RES 552 552 Phosphoserine; by PDPK1.
 MOD_RES 554 554 Phosphoserine; by PHK.
 MOD_RES 579 579 Phosphoserine; by MARK1, BRSK1, BRSK2 and
 MOD_RES 596 596 Deamidated asparagine; in tau and PHF-
 MOD_RES 602 602 Phosphoserine; by PHK.
 MOD_RES 606 606 Phosphoserine; by PHK.
 MOD_RES 610 610 Phosphoserine; by MARK1; in PHF-tau.
 MOD_RES 622 622 Phosphoserine; by MARK1; in PHF-tau.
 MOD_RES 641 641 Phosphoserine; by MARK1; in PHF-tau.
 MOD_RES 669 669 Phosphoserine; by PHK.
 MOD_RES 673 673 Phosphoserine; by MARK1; in PHF-tau.
 MOD_RES 713 713 Phosphoserine; by CK1 and PDPK1.
 MOD_RES 717 717 Phosphoserine; alternate.
 MOD_RES 720 720 Phosphothreonine.
 MOD_RES 721 721 Phosphoserine; by CK1 and PDPK1.
 MOD_RES 726 726 Phosphoserine.
 MOD_RES 729 729 Phosphoserine (By similarity).
 MOD_RES 731 731 Phosphothreonine (By similarity).
 MOD_RES 733 733 Phosphoserine; by CaMK2 and TTBK1.
 MOD_RES 739 739 Phosphoserine; by PDPK1 and TTBK1.
 MOD_RES 744 744 Phosphothreonine; by TTBK1.
 CARBOHYD 87 87 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 383 383 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 467 467 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 480 480 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 491 491 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 525 525 O-linked (GlcNAc...).
 CARBOHYD 542 542 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 551 551 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 555 555 O-linked (GlcNAc...).
 CARBOHYD 576 576 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 597 597 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 598 598 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 664 664 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 670 670 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 686 686 N-linked (Glc) (glycation); in PHF-tau;
 CARBOHYD 717 717 O-linked (GlcNAc...); alternate.
 DISULFID 608 639 By similarity.
 CROSSLNK 571 571 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 628 628 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Alzheimer disease; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Disulfide bond; Glycation; Glycoprotein; Isopeptide bond; Membrane; Microtubule; Neurodegeneration; Parkinsonism; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 758 AA 
Protein Sequence
MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG 60
SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG 120
HVTQARMVSK SKDGTGSDDK KAKGADGKTK IATPRGAAPP GQKGQANATR IPAKTPPAPK 180
TPPSSGEPPK SGDRSGYSSP GSPGTPGSRS RTPSLPTPPT REPKKVAVVR TPPKSPSSAK 240
SRLQTAPVPM PDLKNVKSKI GSTENLKHQP GGGKVQIINK KLDLSNVQSK CGSKDNIKHV 300
PGGGSVQIVY KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI 360
THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV 420
DSPQLATLAD EVSASLAKQG L 441 
Gene Ontology
 GO:0030424; C:axon; IDA:UniProtKB.
 GO:0035085; C:cilium axoneme; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030426; C:growth cone; IDA:UniProtKB.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005875; C:microtubule associated complex; TAS:ProtInc.
 GO:0034399; C:nuclear periphery; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0045298; C:tubulin complex; IDA:UniProtKB.
 GO:0071813; F:lipoprotein particle binding; IPI:UniProtKB.
 GO:0008017; F:microtubule binding; IDA:UniProtKB.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0007628; P:adult walking behavior; IEA:Compara.
 GO:0008088; P:axon cargo transport; IEA:Compara.
 GO:0007409; P:axonogenesis; IEA:Compara.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
 GO:0047497; P:mitochondrion transport along microtubule; IEA:Compara.
 GO:0032387; P:negative regulation of intracellular transport; IEA:Compara.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
 GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
 GO:0010506; P:regulation of autophagy; IGI:MGI.
 GO:0060632; P:regulation of microtubule-based movement; IEA:Compara. 
Interpro
 IPR027324; MAP2/MAP4/Tau.
 IPR001084; Tau/MAP_tubulin-bd_rpt.
 IPR002955; Tau_protein. 
Pfam
 PF00418; Tubulin-binding 
SMART
  
PROSITE
 PS00229; TAU_MAP_1
 PS51491; TAU_MAP_2 
PRINTS
 PR01261; TAUPROTEIN.