Numbering according to the longest isoform of 441 AA (Nomemclature selon l'isoforme la plus longue (441 acides aminés)

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Cartoon / summary / tableau recapitulatif

1 M (Met) (N terminal)

2 A (Ala)

3 E (Glu)

4 P (Pro)

5 R (Arg)

6 Q (Gln)

7 E (Glu)

8 F (Phe)

9 E (Glu)

10 V (Val)

11 M (Met)

12 E (Glu)

13 D (Asp)

14 H (His)

15 A (Ala)

16 G (Gly)

17 T (Thr)

18 Y (Tyr)

19 G (Gly)

20 L (Leu)

21 G (Gly)

22 D (Asp)

23 R (Arg)

24 K (Lys)

25 D (Asp)

26 Q (Gln)

27 G (Gly)

28 G (Gly)

29 Y (Tyr)
- Phosphorylated in Tau-PHFs and after Ab exposure (Williamson et al., 2002)
 

30 T (Thr)

31 M (Met)

32 H (His)

33 Q (Gln)

34 D (Asp)

35 Q (Gln)

36 E (Glu)

37 G (Gly)

38 D (Asp)

39 T (Thr) Phosphorylated by casein kinase II (Greenwood JA et al, 1994)

40 D (Asp)

41 A (Ala)

42 G (Gly)

43 L (Leu)

44 K (Lys) END EXON 1 Fin

intron: gttagtggac..........................

45 E (Glu)

46 S (Ser) Phosphorylated in vitro by Map kinase (signal: RTKs); p38  (Reynolds et al, 2000) and by GSK3b (for review; Billingsley et al 1997; Jonhson et al 1998; Illenberger et al 1998; Godeman et al, 1999)
- Dephosphorylated by PP2B (gong et al., 1994)

47 P (Pro)

48 L (Leu)

49 Q (Gln)

50 T (Thr) Phosphorylated in vitro by Cdc2 (Johnson and Litersky., 1996 ; Illenberger et al., 1998)  MAPK (Roder et al, 1997)  and GSK3b(Illenberger et al 1998; Godeman et al, 1999)
 

51 P (Pro)

52 T (Thr)

53 E (Glu)

54 D (Asp)

55 G (Gly)

56 S (Ser)

57 E (Glu)

58 E

59 P (Pro)

60 G (Gly)

61 S (Ser)

62 E (Glu)

63 T (Thr)

64 S (Ser)

65 D (Asp)

66 A (Ala)

67 K (Lys)

68 S (Ser)

69 T (Thr) Phosphorylated in vitro by MAPK (Roder et al, 1997) and GSK3b (Godeman et al, 1999)

70 P (Pro)

71 T (Thr)

72 A (Ala)

73 E (Glu) End exon 2

74 D (Asp)

75 V (Val)

76 T (Thr)

77 A (Ala)

78 P (Pro)

79 L (Leu)

80 V (Val)

81 D (Asp)

82 E (Glu)

83 G (Gly)

84 A (Ala)

85 P (Pro)

86 G (Gly)

87 K (Lys)

88 Q (Gln)

89 A (Ala)

90 A (Ala)

91 A (Ala)

92 Q (Gln)

93 P (Pro)

94 H (His)

95 T (Thr)

96 E (Glu)

97 I (Ile)

98 P (Pro)

99 E (Glu)

100 G (Gly)

101 T (Thr)

102 T (Thr) End EXON 3 

103 A (Ala)

104 E (Glu)

105 E (Glu)

106 A (Ala)

107 G (Gly)

108 I (Ile)

109 G (Gly)

110 D (Asp)

111 T (Thr)

112 P (Pro)

113 S (Ser)

114 L (Leu)

115 E (Glu)

116 D (Asp)

117 E (Glu)

118 A (Ala)

119 A (Ala)

120 G (Gly)

121 H (His)

122 V (Val)

123 T (Thr)

124 Q (Gln) End exon 4 

125 A (Ala)

126 R (Arg)

127 M (Met)

128 V (Val)

129 S (Ser)

130 K (Lys)

131 Ser

132 K (Lys)

133 D (Asp)

134 G (Gly)

135 T (Thr)

136 G (Gly)

137 Ser

138 D (Asp)

139 D (Asp)

140 K (Lys)

141 K (Lys)

142 A (Ala)

143 K (Lys) End exon5 

144 G (Gly)

145 A (Ala)

146 D (Asp)

147 G (Gly)

148 K (Lys)

149 T (Thr)

150 K (Lys)

151 I (Ile)

152 A (Ala)

153 T (Thr) Phosphorylated in vitro by Cdk5, MAPK, Cdc2  (Illenberger et al, 1998) and GSK3b(Godeman et al, 1999)

154 P (Pro)**

155 R (Arg)

156 G (Gly)

157 A (Ala)

158 A (Ala)

159 P (Pro)

160 P (Pro

161 G (Gly)

162 Q (Gln)

163 K (Lys)

164 G (Gly)

165 E (Glu)

166 A (Ala)

167 N (Asn)

168 A (Ala)

169 T (Thr)

170 R (Arg)

171 I (Ile)

172 P (Pro)

173 A (Ala)

174 K (Lys)

175 T (Thr)
- Phosphorylated in Tau-PHF (Hanger et al., 1998)
- Phosphorylated in vitro by MAPK; p38; JNK and GSK3b (Reynolds et al, 2000)
 

176 P (Pro)

177 P (Pro)

178 A (Ala)

179 P (Pro)

180 K (Lys)

181 T (Thr)      AT270 binding site
- Phosphorylation modulated by calcineurin. (Garver et al Molec. Pharm. 1999, 55:632-641 )
- phosphorylated in vitro by GSK 3b,MAPK; p38; JNK (Reynolds et al., 1997; Godeman et al, 1999 ; Reynolds et al, 2000)
- phosphorylated in vitro by Cdk5, Erk1/2, SAPK1g, SAPK2a, SAPK2b (Reynolds et al, 1997), SAPK3 and SAPK4 (Goedert et al, 1997) and in Cos cells (Buée-Scherrer et al., 2002)
-  phosphorylated by GSK3b in NT2  (Hong et al, 1997) and in SY5Y cells (Xie et al., 1998). LiCl inhibits this phosphorylation in SY5Y cells.
- PKN reduces this phosphorylation in vivo (Taniguchi et al., 2001)

182 P (Pro)

183 P (Pro)

184 S (Ser)
- May be phosphorylated in Tau-PHF (Hanger et al., 1998)
- Phosphorylated in vitro by GSK3 (a+b) (Wang et al, 1998)

185 Ser End exon7
- May be phosphorylated in Tau-PHF (Hanger et al., 1998)
- Phosphorylated in vitro by p38 (Reynolds et al, 2000)

186 G (Gly)

187 E (Glu)

188 P (Pro)

189 P (Pro)

190 K (Lys)

191 S (Ser)

192 G (Gly)

193 D (Asp)

194 R (Arg)

195 Ser
- Phosphorylated by Cdk5 (tau kinase II); Cdc2 (for review ; Billingsley et al 1997;)
- Phosphorylated in vitro by GSK3b+ pKA (Wang et al, 1998)
- Dephosphorylated by PP2A in rat brain slices (Gong et al., 2000)

196 G (Gly)

197 Y (Tyr)

198 S (Ser)
- Phosphorylated in vitro by GSK3b + pKA (Wang et al, 1998)

199 S (Ser)
- Phosphorylated by MAPK, GSK 3b (tau kinase I) (Reynolds et al, 2000),ERK1/2, GSK3b (Illenberger et al, 1998) and GSK3a (Billingsley et al 1997)
- Phosphorylated in COS cells by GSK3b (Michel et al., 1998)
- Dephosphorylated by PP2B (gong et al., 1994) and by PP2A in rat brain slices (Gong et al., 2000)
- Phosphorylated in starved mice (Yanagisawa et al., 1999)

200 P (Pro)

201 G (Gly)

202 S (Ser)  AT8 binding site
- Phosphorylated by GSK 3b (tau kinase I) (Illenberger et al, 1998; Godeman et al, 1999)  in collaboration with CdK5( Ahlijanian et al 2000)
- Phosphorylated in vivo (in mitotic cells) by Cdk5 (tau kinase II) and Cdc2 (Preuss et al, 1998)
- Phosphorylated in vitro by Cdk2 (Baumann et al., 1993), p38 (Reynolds et al, 1997); JNK and Map kinase (Reynolds et al, 2000)
- Phosphorylated by GSK3a (for review ; Billingsley et al 1997)
- Phosphorylated in vitro by pKA + GSK3 (Wang et al, 1998)
- Phosphorylation modulated by Insulin and IGF1 in SY5Y cell line (Lesort et al, 1999)
- Dephosphorylated by PP2B (gong et al., 1994) and by PP2A in rat brain slices (Gong et al., 2000)
- Phosphorylated in COS cells by Cdk5/P25 but not by Cdk5/p35 (Michel et al., 1998; Van den Haute et al., 2001) in transgenic mices.
- Phosphorylated in Cos cells by SAPK (Buée-Scherrer et al., 2002)
- Phosphorylated in starved mice (Yanagisawa et al., 1999)
- PKN reduces this phosphorylation in vivo (Taniguchi et al., 2001)
- Ab (1-42) enhances this phosphorylation site both in vitro and in vivo ( Götz et al., 2001)

203 P (Pro)

204 G (Gly)

205 T (Thr) phosphorylated: AT8 binding site
- Phosphorylated by Cdk5 (tau kinase II); Cdc2 (Ahlijanian et al 2000)
- Phosphorylated in vivo (in mitotic cells) (Preuss et al, 1998)
- Phosphorylated in vitro by Cdk2 (Baumann et al., 1993), GSK 3b (tau kinase I) (Illenberger et al, 1998; Godeman et al, 1999) by p38; JNK, MAPK (Reynolds et al, 1997; Reynolds et al, 2000) and by pKA + GSK3 (Wang et al, 1998)
- Phosphorylation modulated by insulin and IGF1 in SY5Y cell line (Lesort et al, 1999)
- Phosphorylated in COS cells by Cdk5/P25 but not by Cdk5/p35 (Michel et al., 1998; Van den Haute et al., 2001) in transgenic mices
- Phosphorylated in Cos cells by SAPK (Buée-Scherrer et al., 2002)
- Phosphorylated in starved mice (Yanagisawa et al., 1999)
- PKN reduces this phosphorylation in vivo (Taniguchi et al., 2001)
- Ab (1-42) enhances this phosphorylation site both in vitro and in vivo ( Götz et al., 2001)

206 P (Pro)

207 G (Gly)

208 S (Ser)
- Phosphorylated in Tau-PHFs (Morishima-Kawashima, 1995)
- Phosphorylated by TTK : Tau Tubulin Kinase (Tomizawa et al., 2001)
- Phosphorylated by GSK3b if T212 is prephosphorylated by DYRK isoforms (Woods et al., 2001)

209 R (Arg)

210 S (Ser)
- Phosphorylated in Tau-PHFs (Morishima-Kawashima, 1995)
- Phosphorylated by TTK : Tau Tubulin Kinase (Tomizawa et al., 2001)

211 R (Arg)

212 T (Thr) AT100 binding site and Alzheimer disease specific (Maillot et al, 1998)
- Sequential phosphorylation by GSK3b at T212 and by PKA at S214 in presence of polyanions like heparin generates this epitope in vitro (Zheng-Fischhöfer et al, 1997)
- Phosphorylated by PKA, Cdk5  in vitro(Illenberger et al, 1998;)  in presence of heparin (Paudel and Li, 1999)
- Phosphorylated in apoptotic human fetal astrocytes by Cdc2 after Okadaïc acid treatment (Ksiezack-Reding et al., 2000)
- Phosphorylated in vitro by GSK 3b (tau kinase I), p38 (Reynolds et al, 1997), JNK, MAPK  (Reynolds et al, 2000) GSK3a (for review; Billingsley et al 1997) and DYRK isoforms (Woods et al., 2001)

213 P (Pro)

214  S (Ser)  AT100 binding site and Alzheimer disease specific (Maillot et al, 1998) / CP3 binding site (Jicha et al, 1999)
- Important site for Tau tubulin interaction. Phosphorylation provokes dissociation (Schneider et al, Biochemistry, 1999, 38:3549-3558)
- Sequential phosphorylation by GSK3b at T212 and by PKA at S214 in presence of polyanions like heparin generates this epitope in vitro ( Brandt et al, 1994; Zheng-Fischhöfer et al, 1997)
- Phosphorylated in apoptotic human fetal astrocytes by PBK/AKT, after Okadaïc acid treatment (Ksiezack-Reding et al., 2000)
- Phosporylated by GSK 3b (tau kinase I), Cdk5 (Tau kinase II) in vitro (Illenberger et al, 1998), showing that this is a prominent phosphorylation site in metaphase, but not in interphase.
- Phosphorylated by  PKA (early marker of AD) (Scott et al., 1993; Jicha et al, 1999; Johnson and Litersky., 1996)
- This single phosphorylation inhibits PHFs assembly (Schneider et al, 1999)
- If ser214 is phosphorylated, this amino acid is one of the major factors responsive to a decrease of the ability of tau protein to nucleate MTs (Brandt et al, 1994)
- Phosphorylated by PKN (Taniguchi et al., 2001)
- phosphorylation was enhanced by glycosylation (Liu et al., 2002)

215 L (Leu)

216 P (Pro)

217 T (Thr)
- Phosphorylated  in vitro by GSK3b, MAPK, p38 and JNK (Illenberger et al, 1998; Reynolds et al, 2000)

218 P (Pro)

219 P (Pro)

220 T (Thr)

221 R (Arg)

222 E (Glu)

223 P (Pro) End exon8 

224 K (Lys)

225 K (Lys)

226 V (Val)

227 A (Ala)

228 V (Val)

229 V (Val)

230 R (Arg)

231 T (Thr)     AT180/TG3/PHF27 binding site (difference of conformation)
- Phosphorylation modulated by calcineurin. (Garver et al Molec. Pharm. 1999, 55:632-641).
- Phosphorylated by Cdk5 (tau kinase II) Cdc2 in vitro (Illenberger et al, 1998) in the presence of heparin (Paudel and Li, 1999)
- Phosphorylated in situ  (Alzheimer disease) by Cdc2 (Preuss et al, 1998; Lu et al, 1999)
- Phosphorylated in mitotic cells (Vincent et al, 1996)
- Phosphorylated in vitro by GSK 3b (tau kinase I),  p38,  JNK, MAPK (Reynolds et al, 2000) and GSK3 + pKA (Wang et al, 1998)
- Phosphorylated by GSK3a in presence of heparin (Morishima-Kawashima et al, 1995; for review ; Billingsley et al 1997)
- Phosphorylated in NT2 cells (Hong et al, 1997)
- Phosphorylated in COS Cells by GSK 3b . In addition, phosphorylated in these COS Cells by Cdk5/p25 but not by Cdk5/P35 (like in transgenic mices) (Michel et al., 1998; Van den Haute et al., 2001)
- PKN reduces this phosphorylation in vivo (Taniguchi et al., 2001)
 

232 P (Pro)

233 P (Pro)

234 K (Lys)

235 Ser     AT180 binding site (Different conformations)
- Site discovered in mitotic cells (Vincent et al, 1996; Preuss et al, 1998)
- Preferential phosphorylation site of Cdk5 and Cdc2 (Lu et al, 1999)
- Phosphorylated in vitro by P38, JNK, GSK3b, MAPK (Godeman et al, 1999; Reynolds et al, 2000), phosphorylase K (Paudel et al, 1997) and GSK3 + PKA (Wang et al, 1998)
- Phosphorylated by GSK3a (For review; Billingsley et al 1997)
- Preferential site of PP2B (Calcineurin) (Gong et al, 1994)
- Phosphorylated by Cdk5/P25 in COS Cells and in transgenic mices but not by Cdk5/P35 (Michel et al., 1998; Van den Haute et al., 2001)

236 P (Pro)

237 S (Ser)
- Phosphorylated in Tau-PHF (Hanger et al., 1998)
- Phosphorylated by phosphorylase kinase (Paudel et al, 1997)

238 S (Ser)
- Phosphorylated in Tau-PHF (Hanger et al., 1998)

239 A (Ala)

240 K (Lys)

241 S (Ser)

242 R (Arg)

243 L (Leu)

244 Q (Gln)

245 T (Thr)
- Phosphorylated in vitro by p38 (Reynolds et al, 2000) and PKA (Schneider et al, 1999)

246 A (Ala)

247 P (Pro)

248 V (Val)

249 P (Pro)

250 M (Met)

251 P (Pro)

252 D (Asp)

253 L (Leu)

254 K (Lys)

255 N (Asn)

256 V (Val)

257 K (Lys)

258 Ser
- Phosphorylated by PKC and PKN in vitro (Taniguchi et al., 2001)

259 K (Lys)

260 I (Ile)

261 G (Gly)

262 Ser         phosphorylated: 12E8/Ab262 binding site
- Important site for Tau tubulin interaction. Phosphorylation provokes 40% dissociation (Schneider et al, Biochemistry, 1999, 38:3549-3558).
- Phosphorylation induces neuritic outgrowth (Biernat et al, Mol Biol. Cell, 1999,10:727-740)
- PKA-catalyzed phosphorylation, via alpha-synuclein (Jensen et al, 1999; Jonhson and Litersky, 1996)  heparin (Paudel and Li, 1999) and 14.3.3 proteins (Hashiguchi et al., 2000)
- Phosphorylated by  PKA ,  p110 mapk (MARK) (Drewes et al, 1997; Xie et al., 1998), CamK II (Modulation of the phosphorylation by phospholipids) (Baudiert et al, 1987), Phosphorylase kinase (Paudel et al, 1997),  by GSK3a in presence of heparin (Billingsley et al 1997)) and by GSK3 in presence of heparin or tubulin (Moreno et al., 1995)
- Phosphorylated in vitro by PK 35/41 (Biernat et al, 1993) and by GSK3 + pKA (Wang et al, 1998)
- Phosphorylated in vitro by NCLK (P35/Cdk5) in presence of Heparin (Hasegawa et al, 1997)
- Phosphorylation in SY5Y cell line by MARK (Jenkins et al., 2000)
- Dephosphorylated by PP2A in rat brain slices (Gong et al., 2000)
- Ab (1-42) enhances this phosphorylation site both in vitro and in vivo ( Götz et al., 2001)
- Phosphorylation was enhanced by glycosylation (Liu et al., 2002)
-Phosphorylation at this site reduces PHF formation (Schneider et al., 1999)

263 T (Thr) Repeat 1

264 E (Glu)

265 N (Asn)

266 L (Leu)

267 K (Lys)

268 H (His)

269 Q (Gln)

270 P (Pro)*

271 G (Gly)

272 G (Gly)

273 G (Gly)

274 K (Lys) End exon9

276 Q (Gln)

277 I (Ile)

278 I (Ile)

279 N (Asn)

280 K (Lys)

281 K (Lys)

282 L (Leu)

283 D (Asp)

284 L (Leu)

285 S (Ser)
- Phosphorylated by CamK II (Jonhson and Litersky, 1996), phosphorylase kinase (Paudel et al, 1997)

286 N (Asn)

287 V (Val) Repeat 2

288 Q (Gln)

289 S (Ser)

290 K (Lys)

291 C (Cys)

292 G (Gly)

293 S (Ser)
- Phosphorylated by PK 35/41 (Biernat et al, 1993),  MARK (Drewes et al, 1995;Jonhson and Litersky, 1996), pKA and pKC (Drewes et al, 1995; Taniguchi et al., 2001)
- Phosphorylation at this site reduces PHF formation (Schneider et al., 1999)

294 K (Lys)

295 D (Asp)

296 N (Asn)

297 I (Ile)

298 K (Lys)

299 H (His)

300 V (Val)

301 P (Pro)

302 G (Gly)

303 G (Gly)

304 G (Gly)

305 Ser
- Phosphorylated in vitro by p38 (Reynolds et al, 2000), pKA , pKC, MARK (Drewes et al, 1995) and phosphorylase K (Paudel et al, 1997)

-------------------------End exon 10------------------------

Intron that regulates splicing of exon 10 (mutations provoke FTDP-17)

-----------------

306 V (Val)

307 Q (Gln)

308 I (Ile)

309 V (Val)

310 Y (Tyr)

311 K (Lys)

312 P (Pro)** R2-R3 IR

313 V (Val)

314 D (Asp)

315 L (Leu)

316 Ser

317 K (Lys)

318 V (Val) R3

319 T (Thr)

320 Ser
- Phosphorylated in vitro by PKA (Schneider et al, 1999) and MARK in presence of polyanions like Heparin
- This phosphorylation inhibits PHF assembly
- Phosphorylation site in vitro  and in COS Cells for PKN (Taniguchi et al., 2001)
- Dephosphorylated in COS Cells by Calcineurine (PP2B) (Taniguchi et al., 2001)

321 K (Lys)

322 C (Cys)

323 G (Gly)

324 Ser
- The phoshorylation induce the neurite outgrowth (Biernat et al,  1999)
- Phosphorylated by PKA, PKC  (signal: Ca2+/DAG) and MARK (Drewes et al, 1995 ; Billingsley et al 1997;Taniguchi et al., 2001)
- Phosphorylated by GSK3a if Heparin (Moreno et al., 1995; Billingsley et al 1997) and by PK 35/41 (Biernat et al, 1993)
- Phosphorylation at this site reduces PHF formation (Schneider et al., 1999)

325 L (Leu)

326 G (Gly)

327 N (Asn)

328 I (Ile)

329 H (His)

330 H (His)

331 K (Lys)

332 P (Pro)* fin exon 11 

333 G (Gly)

334 G (Gly)

335 G (Gly)

336 Q (Gln) R3-R4 IR

337 V (Val)

339 V (Val)

340 K (Lys)

341 Ser

342 E (Glu)

343 K (Lys) R3-R4 IR

344 L (Leu)

345 D (Asp)

346 F (Phe)

347 K (Lys)

348 D (Asp)

349 R (Arg)

350 V (Val) R4

351 Q (Gln)

352 Ser
- Phosphorylated by phosphorylase kinase (Paudel et al, 1997)
- Phosphorylation site in vitro   for PKN (Taniguchi et al., 2001)
 

353 K (Lys)

354 I (Ile)

355 G (Gly)

356 Ser
- Phosphorylated in Tau-PHF (Hanger et al., 1998)
- PKA-catalyzed phosphorylation, via alpha-synuclein (for review; Billingsley et al 1997; Jensen et al,1999)and 14.3.3 proteins (Hashiguchi et al., 2000)
- Phosphorylated in vitro by p38, JNK (Reynolds et al, 2000), MARK, CamK II, PKA (Jonhson and Litersky, 1996;Xie et al., 1998), GSK3a if heparin (Billingsley et al 1997), Cam KII (Drewes et al, 1995) and PK 35/41 (Biernat et al, 1993)
- Phosphorylation in SY5Y cell line by MARK (Jenkins et al., 2000)
- Phosphorylation at this site reduces PHF formation (Schneider et al., 1999)
- Phosphorylation was enhanced by glycosylation (Liu et al., 2002)

357 L (Leu)

358 D (Asp)

359 N (Asn)

360 I (Ile)

361 T (Thr)
- Phosphorylated by PHF kinase (phosphorylation modulated by PKA) (Jicha et al, 1999)

362 H (His)

363 V (Val)

364 P (Pro)

365 G (Gly)

366 G (Gly)

367 G (Gly)

368 N (Asn)

369 K (Lys)

370 K (Lys) fin exon 12 

371 I (Ile)

372 E (Glu)

373 T (Thr)

374 H (His)

375 K (Lys)

376 L (Leu)

377 T (Thr)
- Phosphorylated by pKC (Steiner (1993)- "Phosphorylation of Tau protein"-Thesis-University of Hamburg)

378 F (Phe)

379 R (Arg)

380 E (Glu)

381 N (Asn)

382 A (Ala)

383 K (Lys)

384 A (Ala)

385 K (Lys)

386 T (Thr)

387 D (Asp)

388 H (His)

389 G (Gly)

390 A (Ala)

391 E (Glu)........................... mAb 423 (truncated tau) Wishick

392 I (Ile)

393 V (Val)

394 Y (Tyr)

395 K (Lys)

396 Ser     Phosphorylated: AD2/PHF1/8D8 binding site
- Site riscovered in mitotic process (Preuss et al, 1998)
- Phosphorylated in vitro by Cdk2 (Baumann et al., 1993), Cdk5, Cdc2, MAPK, GSK3b(Illenberger et al, 1998; Godeman et al, 1999), GSK3a , caseine kinase I and II (Billingsley et al 1997), JNK and by p38 (Reynolds et al, 2000)
- Phosphorylation modulated by insulin in SY5Y cell line (Lesort et al, 1999) or NT2 cells by its modulation of GSK3b (Hong et al, 1997)
- Phosphorylated in COS cells by GSK3b (Michel et al., 1998), SAPK (Buée-Scherrer et al., 2002) and in SY5Y cells (Xie et al., 1998) : LiCl prevents this phosphorylation.
- Phosphorylation at this site is enhanced in proliferating neuroblastoma cells (Pope et al., 1994)
- Dephosphorylated by PP2B (Gong et al, 1994) and by PP2A in rat brain slices (Gong et al., 2000)
- Phosphorylated in starved mice (Yanagisawa et al., 1999)
 

397 P (Pro)**

398 V (Val)

399 V (Val)

400 S (Ser)
- Phosphorylated in vitro by GSK3b (Reynolds et al, 2000)

401 G (Gly)

402 D (Asp)

403 T (Thr) Phosphorylated by GSK3bif S404 is prephosphorylated (Godeman et al, 1999)

404 Ser      Phosphorylated: AD2/PHF1 binding site
- Site riscovered in mitotic process (Preuss et al, 1998)
- Phosphorylated in vitro by Cdk2 (Baumann et al., 1993), Cdk5, Cdc2, MAPK, GSK3b(Illenberger et al, 1998; Godeman et al, 1999), GSK3a, caseine kinase I and II (Billingsley et al 1997) and by p38 (Reynolds et al, 2000)
- Phosphorylation modulated by insulin in SY5Y cell line (Lesort et al, 1999) or NT2 cells by its modulation of GSK3b (Hong et al, 1997). Licl prevents this phosphorylation in SY5Y cells (Xie et al., 1998).
- Phosphorylated by Cdk5/P25 in COS Cells and in transgenic mices but not by Cdk5/P35 (Michel et al., 1998; Van den Haute et al., 2001)
- Phosphorylated by SAPK in COS cells (Buée-Scherrer et al., 2002)
- Dephosphorylated by PP2B (Gong et al, 1994) and by PP2A in rat brain slices (Gong et al., 2000)
- Phosphorylation at this site is enhanced in proliferating neuroblastoma cells (Pope et al., 1994)

405 P (Pro)**

406 R (Arg)

407 H (His)

408 L (Leu)

409 Ser PG5 Binding site
- Phosphorylated by  PKA (early marker of AD) (Jicha et al, 1999)
- Phosphorylated by Cam Kinase II (signal: Ca2+) (For review; Billingsley et al 1997) and by PK35/41 (Biernat et al, 1993)
- Phosphorylation was enhanced by glycosylation (Liu et al., 2002)

410 N (Asn)

411 V (Val)

412 Ser Phosphorylated in  foetal Tau and Tau-PHFs (Morishima-Kawashima, 1995 ; Buee et al, 2000)
- Phosphorylated by PHF kinase (phosphorylation modulated by PKA) (Jicha et al, 1999)

413 Ser - Phosphorylated in vitro by GSK 3b (tau kinase I) (for review;Billingsley et al 1997;Illenberger et al, 1998), and in COS Cells (Michel et al., 1998)
- Phosphorylated in starved mice (Yanagisawa et al., 1999)

414 T (Thr)

415 G (Gly)

416 Ser - Phosphorylated by PKA and CamK II (signal: Ca2+) (Jonhson and Litersky, 1996; for review; Billingsley et al 1997)

417 I (Ile)

418 D (Asp)

419 M (Met)

420 V (Val)

421 D (Asp)

422 Ser  - Phosphorylated: 988/AP422 binding site
- Phosphorylated in vitro by MAPK,  p38, JNK (Reynolds et al, 2000), CamK II (Jonhson et al, 1996) and pKA (Scott et al., 1993; Brandt et al., 1994)
- Phosphorylated by SAPK in COS cells (Buée-Scherrer et al., 2002)
- Dephosphorylated by PP2A in rat brain slices (Gong et al., 2000)
- Phosphorylated in starved mice (Yanagisawa et al., 1999)

423 P (Pro)**

424 Q (Gln)

425 L (Leu)

426 A (Ala)

427 T (Thr)

428 L (Leu)

429 A (Ala)

430 D (Asp)

431 E (Glu)

432 V (Val)

433 Ser

434 A (Ala)

435 Ser

436 L (Leu)

437 A (Ala)

438 K (Lys)

439 Q (Gln)

440 G (Gly)

441 L (Leu)