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sequence
stringlengths
16
117
precursor_charge
int64
1
7
precursor_mz
float64
301
1.8k
mz_array
sequencelengths
6
3.29k
intensity_array
sequencelengths
6
3.29k
experiment_name
stringclasses
1 value
MQNHGYENPTY[UNIMOD:21]K
2
781.307007
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train
SRDPHY[UNIMOD:21]DDFR
3
463.183258
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train
DHLY[UNIMOD:21]STVC[UNIMOD:4]KPR
2
728.324036
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train
SQAKPGTPGGTGGPAPQY[UNIMOD:21]
2
875.887756
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train
HTPY[UNIMOD:21]S[UNIMOD:21]IRC[UNIMOD:4]ER
2
739.784058
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train
AVDGY[UNIMOD:21]VKPQIK
2
649.326172
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train
AVC[UNIMOD:4]STY[UNIMOD:21]LQSR
2
632.769958
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train
VKGEY[UNIMOD:21]DVTVPK
2
657.816833
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train
AVC[UNIMOD:4]STY[UNIMOD:21]LQSR
2
632.769714
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train
GSTAENAEY[UNIMOD:21]LR
2
645.768616
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train
AVC[UNIMOD:4]STY[UNIMOD:21]LQSR
2
632.769348
[ 109.784729, 121.3780289, 133.0422211, 143.1165619, 171.1117096, 248.0689697, 383.6290283, 480.2712402, 503.2953796, 539.2110596, 547.7157593, 548.9968872, 625.2097778, 739.1427612, 746.3144531, 847.3580322, 934.3978882, 935.4071655, 1094.4135742 ]
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train
SLPSGSHQGPVIY[UNIMOD:21]AQLDHSGGHHSDK
3
931.420105
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train
MKGDY[UNIMOD:21]DVTVPK
2
666.795532
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train
AGKGESAGY[UNIMOD:21]MEPYEAQR
3
641.9333
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train
AHAWPSPY[UNIMOD:21]K
2
568.74707
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train
AGKGESAGY[UNIMOD:21]MEPYEAQR
2
962.396606
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train
QLSY[UNIMOD:21]FDRR
2
582.760986
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train
GLPPSNHHAVY[UNIMOD:21]DVPPSVSK
3
694.3298
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train
AHAWPSPY[UNIMOD:21]K
2
568.747009
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train
HTDDEMT[UNIMOD:21]GY[UNIMOD:21]VATR
2
828.289612
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train
VYTY[UNIMOD:21]IQSR
2
555.252441
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train
SESVVY[UNIMOD:21]ADIRK
2
673.818054
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train
AHAWPSPY[UNIMOD:21]K
2
568.747009
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train
SESVVY[UNIMOD:21]ADIRK
3
449.547485
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train
SESVVY[UNIMOD:21]ADIRK
2
673.818176
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train
EVPIY[UNIMOD:21]ANR
2
521.2398
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train
AHAWPSPY[UNIMOD:21]K
2
568.74707
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train
VGEEEHVY[UNIMOD:21]SFPNK
2
807.841309
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train
VGEEEHVY[UNIMOD:21]SFPNK
3
538.896606
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train
AHAWPSPY[UNIMOD:21]K
2
568.747131
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train
GPNVKGEY[UNIMOD:21]DVTMPK
2
807.86084
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train
HADAEMTGY[UNIMOD:21]VVTR
2
765.322693
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train
HYEDGYPGGSDNY[UNIMOD:21]GSLSR
2
1,027.395752
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train
HYEDGYPGGSDNY[UNIMOD:21]GSLSR
2
1,027.3943
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train
EATQPEPIY[UNIMOD:21]AESTK
2
822.358582
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train
DPTNGY[UNIMOD:21]YNVR
2
639.756836
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train
DVLY[UNIMOD:21]SQPPSKPIR
2
790.3927
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train
LATEEPPPRSPPESESEPY[UNIMOD:21]TFSHPNNGDVSSK
3
1,188.1878
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train
VDY[UNIMOD:21]VVVDQQK
2
636.793213
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train
SREYDRLY[UNIMOD:21]EEYTR
3
620.600037
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train
VDY[UNIMOD:21]VVVDQQK
2
636.794128
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train
HVSPVTPPREVPIY[UNIMOD:21]ANR
2
1,006.503845
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train
HVSPVTPPREVPIY[UNIMOD:21]ANR
3
671.3385
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train
VLEDDPEAAY[UNIMOD:21]TTR
2
780.329529
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train
QGY[UNIMOD:21]VIYR
2
489.723206
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train
AHAWPS[UNIMOD:21]PY[UNIMOD:21]K
2
608.730469
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train
REEPEALY[UNIMOD:21]AAVNK
2
785.366638
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train
KVVYENAY[UNIMOD:21]GQFIGPHR
2
979.463135
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train
YVDSEGHLY[UNIMOD:21]TVPIREQGNIYKPNNK
3
1,005.4814
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train
HYEDGYPGGSDNY[UNIMOD:21]GS[UNIMOD:21]LSR
3
711.920898
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train
HYEDGYPGGSDNY[UNIMOD:21]GS[UNIMOD:21]LSR
2
1,067.377319
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train
GESAGY[UNIMOD:21]MEPYEAQR
2
834.318604
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train
HYEDGYPGGSDNY[UNIMOD:21]GS[UNIMOD:21]LSR
3
712.257751
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train
TYYSPVY[UNIMOD:21]R
2
564.738281
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train
GSGDY[UNIMOD:21]MPMSPK
2
625.232056
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train
SSGSGSSVADERVDY[UNIMOD:21]VVVDQQK
3
798.0226
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train
LSSARPGGLGSSSLY[UNIMOD:21]GLGASRPR
3
776.056
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train
TYVDPHTY[UNIMOD:21]EDPNQAVLK
2
1,035.4593
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train
LSSARPGGLGSSSLY[UNIMOD:21]GLGASRPR
4
582.293884
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train
RSDSASSEPVGIY[UNIMOD:21]QGFEK
2
1,018.9475
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train
VSEKPSADY[UNIMOD:21]VLSVR
2
815.39502
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train
RSDSASSEPVGIY[UNIMOD:21]QGFEK
2
1,018.9485
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train
EC[UNIMOD:4]DY[UNIMOD:21]SIDGINR
2
711.773254
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train
LSSARPGGLGSSSLY[UNIMOD:21]GLGASRPR
3
776.0575
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train
DGVY[UNIMOD:21]DVPLHNPPDAK
2
858.881531
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train
AVLY[UNIMOD:21]ADYR
2
525.73468
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train
YSLY[UNIMOD:21]EVHVSGER
2
759.832458
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train
APGSADY[UNIMOD:21]GFAPAAGR
2
744.313416
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train
YLC[UNIMOD:4]EGTESPY[UNIMOD:21]QTGQLHPAIR
3
801.026306
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train
LSSARPGGLGSSSLY[UNIMOD:21]GLGASRPR
3
776.391968
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train
HVSPVT[UNIMOD:21]PPREVPIY[UNIMOD:21]ANR
3
697.994751
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train
EIEY[UNIMOD:21]VETVTSR
2
703.312195
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train
LSSARPGGLGSSS[UNIMOD:21]LY[UNIMOD:21]GLGASRPR
3
802.7117
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train
SESVVY[UNIMOD:21]ADIR
2
609.769775
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train
VLEDDPEATY[UNIMOD:21]TTSGGKIPIR
3
748.022
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train
LSSARPGGLGSSS[UNIMOD:21]LY[UNIMOD:21]GLGASRPR
3
802.7113
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train
VLEDDPEATY[UNIMOD:21]TTSGGKIPIR
2
1,121.5306
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train
TY[UNIMOD:21]VDPHTY[UNIMOD:21]EDPNQAVLK
2
1,075.44397
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train
HAQDY[UNIMOD:21]VLTYNYEGR
2
905.382263
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train
VLEDDPEATY[UNIMOD:21]TTSGGKIPIR
3
748.356323
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train
VLEDDPEATY[UNIMOD:21]TTSGGKIPIR
2
1,122.029053
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train
TY[UNIMOD:21]VDPHTY[UNIMOD:21]EDPNQAVLK
3
717.296753
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train
KVSSTHY[UNIMOD:21]YLLPERPPYLDK
3
796.0621
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train
PGGLGSSSLY[UNIMOD:21]GLGASRPR
3
604.6288
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train
TY[UNIMOD:21]VDPHTY[UNIMOD:21]EDPNQAVLK
3
717.2973
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train
KVSSTHY[UNIMOD:21]YLLPERPPYLDK
3
796.0629
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train
TY[UNIMOD:21]VDPHTY[UNIMOD:21]EDPNQAVLK
2
1,075.4438
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train
LSSARPGGLGSSSLY[UNIMOD:21]GLGASR
3
691.671997
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train
KVSSTHY[UNIMOD:21]YLLPERPPYLDK
2
1,193.5909
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train
YYEGYY[UNIMOD:21]AAGPGYGGR
2
862.34137
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train
ENDY[UNIMOD:21]ESISDLQQGR
2
867.3506
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train
KVSSTHYYLLPERPPY[UNIMOD:21]LDK
4
617.291
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train
KVSSTHY[UNIMOD:21]Y[UNIMOD:21]LLPERPPYLDK
3
822.7189
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train
GVISY[UNIMOD:21]QTLPR
2
607.300659
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train
EVGY[UNIMOD:21]LEFTGPPQKPPR
2
947.957642
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train
IRNLDNGGFY[UNIMOD:21]ISPR
3
567.938721
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train
EVGY[UNIMOD:21]LEFTGPPQKPPR
3
632.3056
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train
VIQPHGGGSNPLEGTQHLQDVPY[UNIMOD:21]VM[UNIMOD:35]VR
3
1,009.148071
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train
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Dataset Card for InstaNovo-P finetuning data

The dataset used for fine tuning InstaNovo-P is comprised of a collection of reprocessed PRIDE projects in Scop3P. (For a list of the projects, see Dataset Sources).

Dataset Details

Dataset Description

The dataset originally contains 4,053,346 PSMs. To only fine-tune on high confidence PSMs, the dataset is filtered at a confidence threshold of 0.80, reducing it to 2,760,939 PSMs, representing 74,686 unique peptide sequences. Most of the data is of human origin, except for PXD005366 and PXD000218, which contain a mix of human and mouse. All PSMs that were used to train the model contained at least one phosphorylated site, while 169, 114 PSMs ( 6%) contained oxidated methionine.

Dataset Structure

To partition the fine-tuning dataset into training, validation and test, GraphPart, an algorithm for homology partitioning, was applied on the set of unique peptide sequences. GraphPart was set to use MMseqs2 with a partitioning threshold of 0.8 and a train-validation-test ratio of 0.7/0.1/0.2 . Of the 74,686 unique sequences, 390 were removed by GraphPart, reducing the total number of PSMs to 2,691,117 in a 2,008,923/232,641/449,553-split, although during training, a random subset of only 2% of the validation set was used in order to reduce computation.

Dataset Sources

PRIDE Accession codes used for training, validation and test sets:

  1. Peng, X. et al. Identification of missing proteins in the phosphoproteome of kidney cancer. J. Proteome Res. 16, 4364–4373, DOI: 10.1021/acs.jproteome.7b00332 (2017).
  2. Post, H. et al. Robust, sensitive, and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons. J. Proteome Res. 16, 728–737, DOI: 10.1021/acs.jproteome.6b00753 (2016).
  3. Tsiatsiani, L. et al. Opposite electron-transfer dissociation and higher-energy collisional dissociation fragmentation characteristics of proteolytic k/r(x)n and (x)nk/r peptides provide benefits for peptide sequencing in proteomics and phosphoproteomics. J. Proteome Res. 16, 852–861, DOI: 10.1021/acs.jproteome.6b00825 (2016).
  4. Espadas, G., BorrΓ s, E., Chiva, C. & SabidΓ³, E. Evaluation of different peptide fragmentation types and mass analyzers in data-dependent methods using an orbitrap fusion lumos tribrid mass spectrometer. PROTEOMICS 17, DOI: 10.1002/pmic. 201600416 (2017).
  5. Bekker-Jensen, D. B. et al. An optimized shotgun strategy for the rapid generation of comprehensive human proteomes. Cell Syst. 4, 587–599.e4, DOI: 10.1016/j.cels.2017.05.009 (2017).
  6. Tran, T. T., Strozynski, M. & Thiede, B. Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in jurkat t cells. PROTEOMICS 17, DOI: 10.1002/pmic.201600470 (2017).
  7. Liu, Z., Wang, F., Chen, J., Zhou, Y. & Zou, H. Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a competitive substitution strategy. J. Chromatogr. A 1461, 35–41, DOI: 10.1016/j.chroma.2016.07.042 (2016).
  8. Humphrey, E. S. et al. Resolution of novel pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling. Mol. Cell. Proteomics 15, 2671–2685 (2016).
  9. Picariello, G. et al. Antibody-independent identification of bovine milk-derived peptides in breast-milk. Food Funct. 7, 3402–3409 (2016).
  10. Francavilla, C. et al. Phosphoproteomics of primary cells reveals druggable kinase signatures in ovarian cancer. Cell Reports 18, 3242–3256, DOI: 10.1016/j.celrep.2017.03.015 (2017).
  11. Lyon, S. M. et al. A method for whole protein isolation from human cranial bone. Anal. Biochem. 515, 33–39, DOI: 10.1016/j.ab.2016.09.021 (2016).
  12. Nguyen, E. V. et al. Hyper-phosphorylation of sequestosome-1 distinguishes resistance to cisplatin in patient derived high grade serous ovarian cancer cells. Mol. amp; Cell. Proteomics 16, 1377–1392, DOI: 10.1074/mcp.m116.058321 (2017).
  13. Drake, J. M. et al. Phosphoproteome integration reveals patient-specific networks in prostate cancer. Cell 166, 1041–1054, DOI: 10.1016/j.cell.2016.07.007 (2016).
  14. Su, N. et al. Special enrichment strategies greatly increase the efficiency of missing proteins identification from regular proteome samples. J. Proteome Res. 14, 3680–3692 (2015).
  15. Creedon, H. et al. Identification of novel pathways linking epithelial-to-mesenchymal transition with resistance to her2-targeted therapy. Oncotarget 7, 11539–11552, DOI: 10.18632/oncotarget.7317 (2016).
  16. van der Mijn, J. C. et al. Evaluation of different phospho-tyrosine antibodies for label-free phosphoproteomics. J. Proteomics 127, 259–263, DOI: 10.1016/j.jprot.2015.04.006 (2015).
  17. Piersma, S. R. et al. Feasibility of label-free phosphoproteomics and application to base-line signaling of colorectal cancer cell lines. J. Proteomics 127, 247–258, DOI: 10.1016/j.jprot.2015.03.019 (2015).
  18. Ruprecht, B. et al. Comprehensive and reproducible phosphopeptide enrichment using iron immobilized metal ion affinity chromatography (fe-imac) columns. Mol. amp; Cell. Proteomics 14, 205–215, DOI: 10.1074/mcp.m114.043109 (2015).
  19. Kauko, O. et al. Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic ras and cip2a signaling. Sci. Reports 5, DOI: 10.1038/srep13099 (2015).
  20. Alpert, A. J., Hudecz, O. & Mechtler, K. Anion-exchange chromatography of phosphopeptides: weak anion exchange versus strong anion exchange and anion-exchange chromatography versus electrostatic repulsion-hydrophilic interaction chromatography. Anal. Chem. 87, 4704–4711 (2015).
  21. Suni, V., Imanishi, S. Y., Maiolica, A., Aebersold, R. & Corthals, G. L. Confident site localization using a simulated phosphopeptide spectral library. J. Proteome Res. 14, 2348–2359 (2015). 17/25
  22. Sharma, K. et al. Ultradeep human phosphoproteome reveals a distinct regulatory nature of tyr and ser/thr-based signaling. Cell Reports 8, 1583–1594, DOI: 10.1016/j.celrep.2014.07.036 (2014).
  23. Tong, J. et al. Integrated analysis of proteome, phosphotyrosine-proteome, tyrosine-kinome, and tyrosine-phosphatome in acute myeloid leukemia. PROTEOMICS 17, DOI: 10.1002/pmic.201600361 (2017).
  24. Bauer, M. et al. Evaluation of data-dependent and -independent mass spectrometric workflows for sensitive quantification of proteins and phosphorylation sites. J. Proteome Res. 13, 5973–5988 (2014).
  25. Shevchuk, O. et al. HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies. J. Proteome Res. 13, 5230–5239 (2014).
  26. Publication pending
  27. Molden, R. C., Goya, J., Khan, Z. & Garcia, B. A. Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination. Mol. amp; Cell. Proteomics 13, 1106–1118, DOI: 10.1074/mcp.o113.036145 (2014).
  28. Rajeeve, V., Vendrell, I., Wilkes, E., Torbett, N. & Cutillas, P. R. Cross-species proteomics reveals specific modulation of signaling in cancer and stromal cells by phosphoinositide 3-kinase (PI3K) inhibitors. Mol. Cell. Proteomics 13, 1457–1470 (2014).
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