2 1 S phase 3 6 SHPARSSSFSRIN T829 S800 KKRRRSDGLAL DGLALSTTDLESE S622 S601 DELVMSPIPTT S

2 1 S phase three 6 SHPARSSSFSRIN T829 S800 KKRRRSDGLAL DGLALSTTDLESE S622 S601 DELVMSPIPTT S25 S1354 PKA, PKD, Aurora, CHK1 CAMK2, PKA 1 two FRKSFSDVRLA ELRIDSSKTLP S1054 CK1, GSK3, CAMK2, PKA, PKG, PKC, CDK5 ten 1 9 CK1, CDK1, MAPK SGVLESNLSPKLTS S741 PKCDescriptionPeptide counts Sequence Kinase predictionPhosphoepitopeHighest detection in S or M phase# TM DomainsSignalP PredictionPLOS A single | www.plosone.orgYes YesTAHypotheticalTAHypotheticalTAHypotheticalTAABC transporterTAPTATaSPTACation transporting ATPaseTAcdp-diacylglycerol synthaseTAHypotheticalTAHypotheticalTAHypotheticalPhosphorylation of Theileria annulata Schizont Surface ProteinsTAHypotheticalPhosphorylation of Theileria annulata Schizont Surface ProteinsYes/signal anchorSignalP PredictionYes# TM DomainsKinase predictionHighest detection in S or M phase0 CDK1 CK1, PKC, CDKALKCDK1, MAPKYesPhospho-epitopes indicated in bold had been those located more abundantly in samples from M- or S-phase (p,0.05). doi:10.1371/journal.pone.0103821.tPhosphoepitopePeptide countsFigure 7. Schematic overview showing all phosphorylated internet sites detected on A) TaSP (TA17315) and B) p104 (TA08425). Detected phosphorylation internet sites are indicated together with the amino acid number. White circles (P) represent phosphorylation web-sites detected in each mitotic and S-phase samples. Grey circles (P) represent phosphorylation web-sites with a important distinction in abundance involving S-phase and mitotic samples. TaSP: schematic topology as predicted by TMpred: 1st TM: 3-21 aa; 2nd TM: 205-223 aa and 3rd TM 262-288 aa. Two phosphorylated serines (S303 and S305) within the Cterminal domain have been more very phosphorylated in S-phase schizontsamples (p,0.01). p104 is predicted to possess a GPI-anchor (GPI). Phosphorylation of 4 serines (S601, S607, S800 and S802) was drastically increased in S-phase when when compared with mitosis. doi:ten.Isorhamnetin Purity 1371/journal.pone.0103821.gYSSS27 SGLHESSCNSTPREGPKFEASPKLLIKNTEASPKTIMSAKPGYSIIKVSequenceSJNK, and if so, regardless of whether this could contribute to sustaining the transformed phenotype. In our preceding function we showed by gel shift assay that endogenous p104 is highly phosphorylated in unsynchronised cell cultures (which mainly consist of cells in G0-G1-phase, Figure S4A), with a slight enhance in the overall phosphorylation of p104 detected in mitotic cells [25]. Because the interaction of lots of plus finish tracking proteins with EB1 is regulated by phosphorylation within the vicinity from the SxIP motif, we focused in detail on a quick fragment (p10452134) that encompasses the EB1-binding domain and 21 potentially phosphorylated sites (dashed underlined in Figure S4).GLP-1R agonist 2 In Vitro We showed that this brief fragment, just like the endogenous protein, is phosphorylated and that in this case the “up-shift” observed in mitotic cells compared to unsynchronised cells was extremely striking.PMID:24406011 This indicated to us that this region is subjected to comprehensive cell cycle-dependent regulation of phosphorylation. We went on to show that CDK1 activity is partially,SfiI-subtelomeric fragment associated proteinDescriptiondynamin-like proteinTable 1. Cont.AccessionTAPLOS A single | www.plosone.orgTATAHypotheticalPhosphorylation of Theileria annulata Schizont Surface Proteinsbut not completely, responsible for phosphorylating p104 for the duration of mitosis. In our existing work, we identified 3 phosphorylated serines inside this fragment, and show that two of them (S601 and S607) are in reality highly phosphorylated during S-phase (Figure 7 and S7, Table S6). With each other, the data fr.