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PXD001681

PXD001681 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleHA-mSLX4 wild type and SIMdependent interactors
DescriptionSUMOylation is known to play important roles in the DNA damage response, however, a role for SUMOylation in interstrand crosslink repair remains enigmatic. We report on the regulation of the SLX4 nuclease scaffold protein by SUMOylation. SLX4 contains three SUMO-Interaction Motifs (SIMs). Mutating all three SIMs abrogated the binding of SLX4 to SUMO-2 and covalent SLX4 SUMOylation. We attempt to identify which protein interaction are SIM dependent.
HostingRepositoryPRIDE
AnnounceDate2015-03-02
AnnouncementXMLSubmission_2015-03-02_06:51:59.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterRomán González-Prieto
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606; scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationListmonohydroxylated residue; acetylated residue; phosphorylated residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02015-01-15 01:55:22ID requested
12015-03-02 06:52:01announced
Publication List
Gonz, á, lez-Prieto R, Cuijpers SA, Luijsterburg MS, van Attikum H, Vertegaal AC, SUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites. EMBO Rep, 16(4):512-9(2015) [pubmed]
Keyword List
curator keyword: Biomedical, Biological
submitter keyword: SLX4, SUMO, Ubiquitin, DNA Repair, Fanconi Anemia
Contact List
Alfred C O Vertegaal
contact affiliationDepartment of Molecular Cell Biology, Leiden University Medical Center, Leiden, the Netherlands.
contact emailA.C.O.Vertegaal@lumc.nl
lab head
Román González-Prieto
contact affiliationLeiden University Medical Center (LUMC)
contact emailR.Gonzalez_Prieto@lumc.nl
dataset submitter
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Dataset FTP location
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