Dataset from the global phosphoproteomic mapping of early mitotic exit in human cells

Data in Brief

Volumn 5, Issue , 2015, Pages 45-52

  Rogers, Samuel ^a   McCloy, Rachael A ^a   Parker, Benjamin L ^b   Chaudhuri, Rima ^b   Gayevskiy, Velimir ^a   Hoffman, Nolan J ^b   Watkins, D Neil ^a,c,d   Daly, Roger J ^e   James, David E ^b   Burgess, Andrew ^a,e  

^a GARVAN INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b UNIVERSITY OF SYDNEY   (Australia)

^c UNIVERSITY OF NEW SOUTH WALES   (Australia)

^d ST VINCENT S HOSPITAL   (Australia)

^e MONASH UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; PHOSPHORYLATION; SUBSTRATES;

'CURRENT; HIGH CONFIDENCE; HUMAN CELLS; PHOSPHOPROTEOMICS; PHOSPHORYLATION SITES; POTENTIAL SUBSTRATE; PREDICTION-BASED; SERINE RESIDUES; SINGLE-CELL LEVEL; TEMPORAL PHOSPHORYLATION;

PHOSPHATASES;

EID: 84940769949     PISSN: None     EISSN: 23523409     Source Type: Journal    
DOI: 10.1016/j.dib.2015.08.010     Document Type: DP

References (13)

1. McCloy R.A., Parker B.L., Rogers S., Chaudhuri R., Gayevskiy V., Hoffman N.J., et al. Global phosphoproteomic mapping of early mitotic exit in human cells identifies novel substrate dephosphorylation motifs. Mol. Cell Proteom. 2015, 14:2194-2212. 10.1074/mcp.M114.046938.
2. Sharma K., D'Souza R.C.J., Tyanova S., Schaab C., Wiśniewski J.R., Cox J., et al. Ultradeep human phosphoproteome reveals a distinct regulatory nature of tyr and ser/thr-based signaling. Cell Rep. 2014, 8:1583-1594. 10.1016/j.celrep.2014.07.036.
3. Bouchoux C., Uhlmann F. A quantitative model for ordered cdk substrate dephosphorylation during mitotic exit. Cell 2011, 147:803-814. 10.1016/j.cell.2011.09.047.
4. Larsen M.R., Thingholm T.E., Jensen O.N., Roepstorff P., Jørgensen T.J.D. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteom. 2005, 4:873-886. 10.1074/mcp.T500007-MCP200.
5. Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127:635-648. 10.1016/j.cell.2006.09.026.
6. Cox J., Neuhauser N., Michalski A., Scheltema R.A., Olsen J.V., Mann M. Andromeda: a peptide search engine integrated into the MaxQuant environment. J. Proteom. Res. 2011, 10:1794-1805. 10.1021/pr101065j.
7. Vizcaíno J.A., Côté R.G., Csordas A., Dianes J.A., Fabregat A., Foster J.M., et al. The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013. Nucleic Acids Res. 2013, 41:D1063-9. 10.1093/nar/gks1262.
8. Baker P.R., Chalkley R.J. MS-viewer: a web-based spectral viewer for proteomics results. Mol. Cell. Proteom. 2014, 13:1392-1396. 10.1074/mcp.O113.037200.
9. Ritchie M.E., Phipson B., Wu D., Hu Y., Law C.W., Shi W., et al. Limma powers differential expression analyses for RNA-sequencing and microarray studies. Nucleic Acids Res. 2015, 43:e47. 10.1093/nar/gkv007.
10. Horn H., Schoof E.M., Kim J., Robin X., Miller M.L., Diella F., et al. KinomeXplorer: an integrated platform for kinome biology studies 2014, 11:603-604. Nat. Methods. 10.1038/nmeth.2968.
11. Colaert N., Helsens K., Martens L., Vandekerckhove J., Gevaert K. Improved visualization of protein consensus sequences by iceLogo. Nat. Methods 2009, 6:786-787. 10.1038/nmeth1109-786.
12. Crooks G.E., Hon G., Chandonia J.-M., Brenner S.E. WebLogo: a sequence logo generator. Genome Res. 2004, 14:1188-1190. 10.1101/gr.849004.
13. McCloy R.A., Rogers S., Caldon C.E., Lorca T., Castro A., Burgess A. Partial inhibition of Cdk1 in G 2 phase overrides the SAC and decouples mitotic events. Cell Cycle 2014, 13:1400-1412. 10.4161/cc.28401.