Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cell surface proteome in HEK293T cells

ABSTRACT: Here, using proteomic analysis of HEK293T cells in which components of the Retriever, CCC, or WASH complexes were knocked out, we provide a data-rich resource that reveals novel molecular insights into how these complexes regulate the membrane proteome.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Kohji Kato

LAB HEAD: Peter J. Cullen

PROVIDER: PXD064873 | Pride | 2026-05-05

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	070922_n1_Fraction_1.raw	Raw
	070922_n1_Fraction_2.raw	Raw
	070922_n1_Fraction_3.raw	Raw
	070922_n1_Fraction_4.raw	Raw
	070922_n1_Fraction_5.raw	Raw

Items per page:

1 - 5 of 19

Similar Datasets

Cell surface proteome in MC3T3-E1 mouse osteoblast cells

Project description:Here, using proteomic analysis of MC3T3-E1 cells subjected to either sh-SCR control or sh-Snx17 knockdown, we provide a data-rich resource that reveals novel molecular insights into how SNX17 regulates the membrane proteome.

2026-05-05 | PXD064783 | Pride

Cell surface proteome in rat cortical neuron

Project description:Here, using proteomic analysis of primary rat cortical neurons subjected to either sh-SCR control or sh-Vps35l knockdown, we provide a data-rich resource that reveals novel molecular insights into how VPS35Lregulates the membrane proteome.

2026-05-05 | PXD064824 | Pride

Interactome of DPYSL5 protein in H4 cells

Project description:Here, using interactome analysis of DPYSL5 protein expressed in H4 cells, we provide a data-rich resource that reveals novel molecular insights into how DPYSL5 interact with associated proteins. Furthermore, by analyzing mutant forms of DPYSL5 identified in patients, we offer insights into how these mutations confer pathogenicity.

2026-05-05 | PXD064831 | Pride

Interactome of COMMD4 and COMMD9 protein in H4 cells

Project description:Here, using interactome analysis of COMMD4 and COMMD9 proteins expressed in H4 cells, we provide a data-rich resource that reveals novel molecular insights into how COMMD4 and COMMD9 interact with associated proteins. Furthermore, by analyzing mutant forms of COMMD4 and COMMD9 identified in patients, we offer insights into how these mutations confer pathogenicity.

2026-05-05 | PXD064827 | Pride

Synaptosome analysis Vps35l conditional knock-out mouse

Project description:Here, using synaptosome analysis of Vps35l-cKOSynapsin1, we provide a data-rich resource that reveals novel molecular insights into how VPS35L work in synapse.

2026-05-05 | PXD064880 | Pride

Comparative LC-MSMS Analysis of Extracellular Vesicles Extracted from Mouse Caecum in Fasted vs. Fed Mice

Project description:Bacterial extracellular vesicles (BEVs) produced by members of the intestinal microbiota can contribute not only to digestion but also mediate microbe-host cell communication via the transfer of functional biomolecules to mammalian host cells. An unresolved question is what host factors and conditions influence BEV cargoes and how do they impact on host cell function? To address this question, we analysed and compared the proteome of BEVs released by the major human gastrointestinal tract (GIT) symbiont Bacteroides thetaiotaomicron (Bt) in vivo in fed versus fasted animals using nano-liquid chromatography with tandem mass spectrometry (LC-MSMS). Among the proteins whose abundance was negatively affected by fasting, nine of ten proteins of the serine protease family, including the regulatory protein dipeptidyl peptidase-4 (DPP-4), were significantly decreased in BEVs produced in the GIT of fasted animals. Strikingly, in ex-tracellular vesicles produced by the intestinal epithelium of the same fasted mice, the proteins with the most increased abundance were serine protease inhibitors (serpins). Together, these findings suggest a dynamic interaction between GI bacteria and the host. Additionally, they indicate a regulatory role for the host in determining the balance be-tween bacterial serine proteases and host serpins exported in bacterial and host extra-cellular vesicles.

2025-05-26 | PXD062737 | Pride

Mass spectrometry of immunoprecipitations from control and Er blood group

Project description:Immunoprecipitates were prepared from test Er(a+b-) donor RBCs and negative control Er(a-b+) (P1) RBCs using anti-Era plasma from P3 (5:1 ratio of plasma to cells) and proteomic analysis was performed.

2024-01-26 | PXD035013 | Pride

ChAdOx infection of human cell lines A549 MRC-5

Project description:Total proteome and phospho proteome of two human cell lines infected with the ChAdOx1 nCoV-19 virus over 72 hours

2021-01-11 | PXD023286 | Pride

Human Platelet PIP3 Signalosome

Project description:Platelets are small, anucleate cells that play an essential role in haemostasis, but can contribute critically to the pathogenesis of cardiovascular disease. Platelets express all four Class I Phosphoinositide 3-kinase (PI3K) isoforms, with previous work revealing important roles for these enzymes in regulating platelet priming, activation and stable thrombus formation. Despite this, detailed mechanistic understanding of how these lipid kinases orchestrate these roles in platelets is limited. Class I PI3Ks predominantly regulate cell function through their catalytic product, the signalling phospholipid phosphatidylinositol-3,4,5-trisphosphate (PIP3), which coordinates the localisation and/or activity of a diverse range of binding proteins. The complete repertoire of these Class I PI3K effectors in platelets remains unknown, hampering current understanding of Class I PI3K-mediated regulation of platelet function. We therefore conducted a global, unbiased screen for PIP3-binding proteins in human platelets using affinity capture coupled to high resolution proteomic mass spectrometry. Thus, we present the first in depth analysis of the PIP3 signalosome of human platelets, revealing an extensive PIP3 interactome, including many proteins previously uncharacterised in this cell type. This work provides important new insights into how Class I PI3K shapes human platelet function.

2017-06-06 | PXD003777 | Pride

General anaesthesia leads to phosphoproteome changes in proteins involved in cytoskeleton remodelling and synaptic processes in the supraoptic nucleus of the hypothalamus

Project description:Despite the widespread use of general anaesthetics, the mechanisms mediating their effects are still not understood. Although suppressed in most parts of the brain, neuronal activity, as measured by FOS activation, is increased in the hypothalamic supraoptic nucleus (SON) by numerous general anaesthetics, and evidence points to this brain region being involved in the induction of general anaesthesia and natural sleep. Posttranslational modifications of proteins, including changes in phosphorylation, enable fast modulation of protein function which could be underlying the rapid effects of general anaesthesia. In order to identify potential phosphorylation events in the brain mediating general anaesthesia effects, we have explored the phosphoproteome responses in the rat SON, and compared these to cingulate cortex (CC) which displays no FOS activation is response to general anaesthetics. We found many changes in the phosphoproteomes of both the CC and SON in response to 15 minutes of isoflurane exposure. Pathway analysis indicated that proteins undergoing phosphorylation adaptations are involved in cytoskeleton remodelling and synaptic signalling events. Importantly, changes in protein phosphorylation appeared to be brain region-specific suggesting that differential phosphorylation adaptations might underlie the different neuronal activity responses to general anaesthesia between the CC and SON. In summary, these data suggest that rapid posttranslational modifications in proteins involved in cytoskeleton remodelling and synaptic signalling events might mediate the central mechanisms mediating general anaesthesia.

2024-01-23 | PXD039391 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data