A comprehensive compilation of SUMO proteomics

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A comprehensive compilation of SUMO proteomics. / Hendriks, Ivo A; Vertegaal, Alfred C O.

In: Nature Reviews. Molecular Cell Biology, Vol. 17, No. 9, 09.2016, p. 581-95.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hendriks, IA & Vertegaal, ACO 2016, 'A comprehensive compilation of SUMO proteomics', Nature Reviews. Molecular Cell Biology, vol. 17, no. 9, pp. 581-95. https://doi.org/10.1038/nrm.2016.81

APA

Hendriks, I. A., & Vertegaal, A. C. O. (2016). A comprehensive compilation of SUMO proteomics. Nature Reviews. Molecular Cell Biology, 17(9), 581-95. https://doi.org/10.1038/nrm.2016.81

Vancouver

Hendriks IA, Vertegaal ACO. A comprehensive compilation of SUMO proteomics. Nature Reviews. Molecular Cell Biology. 2016 Sep;17(9):581-95. https://doi.org/10.1038/nrm.2016.81

Author

Hendriks, Ivo A ; Vertegaal, Alfred C O. / A comprehensive compilation of SUMO proteomics. In: Nature Reviews. Molecular Cell Biology. 2016 ; Vol. 17, No. 9. pp. 581-95.

Bibtex

@article{cd2269e6c6324a08accd55bc915f1d81,
title = "A comprehensive compilation of SUMO proteomics",
abstract = "Small ubiquitin-like modifiers (SUMOs) are essential for the regulation of several cellular processes and are potential therapeutic targets owing to their involvement in diseases such as cancer and Alzheimer disease. In the past decade, we have witnessed a rapid expansion of proteomic approaches for identifying sumoylated proteins, with recent advances in detecting site-specific sumoylation. In this Analysis, we combined all human SUMO proteomics data currently available into one cohesive database. We provide proteomic evidence for sumoylation of 3,617 proteins at 7,327 sumoylation sites, and insight into SUMO group modification by clustering the sumoylated proteins into functional networks. The data support sumoylation being a frequent protein modification (on par with other major protein modifications) with multiple nuclear functions, including in transcription, mRNA processing, DNA replication and the DNA-damage response.",
keywords = "Journal Article",
author = "Hendriks, {Ivo A} and Vertegaal, {Alfred C O}",
year = "2016",
month = sep,
doi = "10.1038/nrm.2016.81",
language = "English",
volume = "17",
pages = "581--95",
journal = "Nature Reviews. Molecular Cell Biology",
issn = "1471-0072",
publisher = "nature publishing group",
number = "9",

}

RIS

TY - JOUR

T1 - A comprehensive compilation of SUMO proteomics

AU - Hendriks, Ivo A

AU - Vertegaal, Alfred C O

PY - 2016/9

Y1 - 2016/9

N2 - Small ubiquitin-like modifiers (SUMOs) are essential for the regulation of several cellular processes and are potential therapeutic targets owing to their involvement in diseases such as cancer and Alzheimer disease. In the past decade, we have witnessed a rapid expansion of proteomic approaches for identifying sumoylated proteins, with recent advances in detecting site-specific sumoylation. In this Analysis, we combined all human SUMO proteomics data currently available into one cohesive database. We provide proteomic evidence for sumoylation of 3,617 proteins at 7,327 sumoylation sites, and insight into SUMO group modification by clustering the sumoylated proteins into functional networks. The data support sumoylation being a frequent protein modification (on par with other major protein modifications) with multiple nuclear functions, including in transcription, mRNA processing, DNA replication and the DNA-damage response.

AB - Small ubiquitin-like modifiers (SUMOs) are essential for the regulation of several cellular processes and are potential therapeutic targets owing to their involvement in diseases such as cancer and Alzheimer disease. In the past decade, we have witnessed a rapid expansion of proteomic approaches for identifying sumoylated proteins, with recent advances in detecting site-specific sumoylation. In this Analysis, we combined all human SUMO proteomics data currently available into one cohesive database. We provide proteomic evidence for sumoylation of 3,617 proteins at 7,327 sumoylation sites, and insight into SUMO group modification by clustering the sumoylated proteins into functional networks. The data support sumoylation being a frequent protein modification (on par with other major protein modifications) with multiple nuclear functions, including in transcription, mRNA processing, DNA replication and the DNA-damage response.

KW - Journal Article

U2 - 10.1038/nrm.2016.81

DO - 10.1038/nrm.2016.81

M3 - Journal article

C2 - 27435506

VL - 17

SP - 581

EP - 595

JO - Nature Reviews. Molecular Cell Biology

JF - Nature Reviews. Molecular Cell Biology

SN - 1471-0072

IS - 9

ER -

ID: 165179558