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. Author manuscript; available in PMC: 2014 Oct 2.
Published in final edited form as: Parasitology. 2014 Feb 21;141(9):1138–1147. doi: 10.1017/S0031182014000055

Table 1.

PTMs of T. gondii, yeast and human Hsp90 members

TgHsp90 YHsp90 HuHsp90α HuHsp90β Domain
Phosphorylation T5 N domain
T7
T23 T22 T36 T31
Y25 Y24 Y38 Y33
Y48 Y47 Y61 Y56
S49 S63 S58
T52 S51 T65 T60
S68 S63
T58 T72 T67
T75 T88 T83
T77 T90 T85
Y186 Y184 Y197 Y192
S200 S198 S211 S206
T220 S231 S226 Linker
S222
S252
S263 S255
S282 Middle domain
T282 T285 T305 T297
Y286 Y289 Y309 Y300
S292 S295 S315 S307
T294 S297 T317 T309
T331 S334
S376 S379 S399 S391
T430 T433 S453 S445
S460 S452
S445 S450 S470 S462
S453 S456 S476 S468
S464
Y469 Y472 Y492 Y484
Y470 Y473 Y493 Y485
S482 S485 S505 S497
S532
Y581 Y604 Y596 C domain
S600 S602 S623
Y604 Y606 Y627 Y619
S616
S619
S654 S657 S677 S668
S663 T683 T675
T725
S726 S718
Acetylationa K271 K274 K294 K286
K384 K387 K407 K399
K559 K582 K574
S-nitrosylation C549 (ND) C572 C564
C574 (ND) C597 C589
a

Data only include acetylated lysines identified in T. gondii and human Hsp90. Other lysines that were detected in human Hsp90 are not included.

ND: indicates not determined; Normal font: PTMs identified; italic font: orthologue residue; –: non phosphorylated (Y,T, S), acetylated (K) or S-nitrosylated (C) residue; Obs.: Hsp90 domains are only identified for phosphorylation section.