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Table 1 The secondary structure prediction in the known PKCK2 phosphorylation sites (S/T-X-X-D/E) in protein substrates. H represents prediction of helix and – represent no prediction of helix or β-sheet. Prediction by both PHD and JPRED methods have been shown in those cases with difference in the secondary structure prediction.

From: Structural basis of regulation and substrate specificity of protein kinase CK2 deduced from the modeling of protein-protein interactions

Protein

Secondary structure prediction at the S/T-X-X-D/E motif

Acetyl Co-A

 

---HH

Clatharin

11,13

----, ----

EF

90

--HH

Hsp90 (beta)

226, 255

--HH, ----

Hsp90 (alpha)

236,263

---H, ---H

EIF

 

----

Ck2β

 

----

DRAPP32

42,45,102

----, ----, ----

HPr E7

31,32

----, ----

Troponin T

1

----

Glycogen synthase

657

----

PKA RII

74,76

----

HMG14

89

----

Myosin light chain

 

--HH (PHD) -HHH(JPRED)

ODC

297,303

----, ----

Ppi

87,120,121

----

Calmodulin

81/79,101

HHHH, --HH

MDM2

267

----

P53

392

----

Eif 2 beta

2,67

----, -HHH

C8 subunit of MCP

243, 250

HHHH, ----

eIF5

387, 388

----,----

FCP1

457

----

Movement protein of TMV

256,261

----, ----

CDC25B

186,187

----, ----

FMR1

406

----

PTEN

370,385

----, ----

Mengovirus leader protein

47

----

β arrestin 2

383

--HH (JPRED) ----(PHD)

Cyclin H

315

----

UBC3B

233

----

Topoisomerase II α

1342

----

Rotavirus NSP5

153,155,163,165

----, ----, ----, ----

TF III A

16

----

HIV1 Rev

5,8

---- (JPRED) HHHH (PHD), -HHH (JPRED) HHHH(PHD)

HDAC1

421,423

----(JPRED) ---H (PHD), ----(JPRED) HHHH (PHD)

CDC34

203,222,231,233,236

----, ----, ----, ----, ----

eIF epsilon

712,713

----, ----

FAF1

289,291

----, ----

VIPR-RP

69,71,110

----, ----(JPRED) --HH(PHD), ----

NDPKA

122

--HH