⮝ Full datasets listing

PXD013332

PXD013332 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleInteractome of the autoimmune risk gene product ANKRD55
DescriptionThe ankyrin repeat domain-55 (ANKRD55) gene contains intronic single nucleotide polymorphisms (SNPs) associated with risk to contract multiple sclerosis, rheumatoid arthritis or other autoimmune disorders. Risk alleles of these SNPs are associated with higher levels of ANKRD55 in CD4+ T cells. The biological function of ANKRD55 is unknown, but given that ankyrin repeat domains constitute one of the most common protein-protein interaction platforms in nature, it is likely to function in complex with other proteins. Thus, identification of its protein interactomes may provide clues. We identified ANKRD55 interactomes via recombinant overexpression in HEK293 or HeLa cells and mass spectrometry of individual co-purified bands or entire gel slabs with subtraction of mock interactomes. 148 specifically interacting proteins were found in total protein extracts and 22 in extracts of sucrose gradient-purified nuclei. Bioinformatic analysis suggested that the ANKRD55‐protein partners from total protein extracts were related to nucleotide and ATP binding, enriched in nuclear transport terms and associated with cell cycle and RNA, lipid and amino acid metabolism. The enrichment analysis of the ANKRD55‐protein partners from nuclear extracts is related to sumoylation, RNA binding, processes associated with cell cycle, RNA transport, nucleotide and ATP binding, among others. The interaction between overexpressed ANKRD55 isoform 001 and endogenous RPS3, the cohesins SMC1A and SMC3, CLTC, PRKDC, VIM, β-tubulin isoforms, and 14-3-3 isoforms were validated by western blot or confocal microscopy. We also identified three phosphorylation sites in ANKRD55, with S436 exhibiting the highest score as likely 14-3-3 binding phosphosite. Our study suggests that ANKRD55 may exert function(s) in the formation or architecture of multiple protein complexes, and is regulated by (de)phosphorylation reactions. Based on interactome and subcellular localization analysis, ANKRD55 is likely transported into the nucleus by the classical nuclear import pathway and is involved in mitosis, probably via effects associated with mitotic spindle dynamics.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_03:59:06.217.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterFelix Elortza
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListphosphorylated residue
InstrumentSynapt MS; LTQ Orbitrap
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-04-01 05:54:24ID requested
12019-09-25 10:53:41announced
22019-10-25 05:55:59announced2019-10-25: Updated publication reference for PubMed record(s): 31620119.
32024-10-22 03:59:14announced2024-10-22: Updated project metadata.
Publication List
Ugidos N, Mena J, Baquero S, Alloza I, Azkargorta M, Elortza F, Vandenbroeck K, Interactome of the Autoimmune Risk Protein ANKRD55. Front Immunol, 10():2067(2019) [pubmed]
10.3389/fimmu.2019.02067;
Keyword List
submitter keyword: ANKRD55, ankyrin repeat, multiple sclerosis, rheumatoid arthritis, autoimmune
Contact List
Felix Elortza
contact affiliationProtemics Service, CIC bioGUNE, Zamudio, Spain
contact emailfelortza@cicbiogune.es
lab head
Felix Elortza
contact affiliationProteomics Platform
contact emailfelortza@cicbiogune.es
dataset submitter
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/09/PXD013332
PRIDE project URI
Repository Record List
[ + ]