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. 2007 May 11;2:49–65.

Table 1.

Putative proteins that may phosphorylate YB-1 at Ser, Thr, and Tyr suggested by the Motif Scanning Prediction Tool.

YB-1 Domain Residue Pitative Regulatory Protein Percentile1
AP-rich N-Term Ser 3 Casein Kinase 2 3.764
Thr 7 DNA PK 0.846
ATM kinase 4.202
Ser 21 GSK3 Kinase2 3.336
Thr 29 PKC δ 0.806
Ser 32 Casein Kinase 1 4.315
Ser 36 Erk 1 Kinase 2 3.248
cold shock domain Thr 62 PKC δ 2.773
PKC α/β/γ 4.452
PKC θ 4.964
Thr 80 DNA PK 2.965
Thr 89 Calmodulin dependent kinase2 2.786
PKC θ 4.964
Ser 102 Akt kinase3 2.703
Ser 102 PKC ε 3.527
Glu 107 PDZ (nNOS)class 3 1.003
Thr 108 DNAPK 3.529
Casein kinase 2 3.764
c-term Tyr 162 Grb2 SH2 2.274
Ser 167 ATM kinase 4.812
Ser 176 14-3-3 1.029
Casein kinase 2 2.023
Tyr 197 Shc PTB 3.945
p85 SH2 4.884
Tyr 208 Abl SH2 0.292
Crk SH2 1.209
Itk SH2 2.124
Nck SH2 2.092
Grb2 SH2 2.983
Thr 271 DNA PK 1.761
ATM kinase 2.342
Tyr 287 Shc PTB 3.170
Ser 314 Casein kinase 2 2.775
1

Given by the Motif scanning prediction tool, the percentile tells how the protein ranks by comparing with all vertebrate proteins in Swiss-Prot, the sequence surrounding that site, and the solvent accessibility at that position.

2

Phosphorylation of YB-1 by GSK3 and ERK2 has been demonstrated by Coles et al. 2005.

3

Phosphorylation of YB-1 by Akt has been shown by Sutherland et al. 2005 and Evdokimova et al. 2006.