Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteome analysis of affinity-purified protein co-precipitates

ABSTRACT: HBO1-MLL interaction promotes AF4/ENL/P-TEFb-mediated leukemogenesis

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Akihiko Yokoyama

PROVIDER: PXD027400 | JPOST Repository | Tue Aug 31 00:00:00 BST 2021

REPOSITORIES: jPOST

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	PM_HA.mzid	Mzid
	PM_HA.raw	Raw
	PM_HA_CID_%5BNode_07%5D.mgf	Mgf
	Vector.mzid	Mzid
	Vector.raw	Raw

Items per page:

1 - 5 of 9

Publications

HBO1-MLL interaction promotes AF4/ENL/P-TEFb-mediated leukemogenesis.

Takahashi Satoshi S Kanai Akinori A Okuda Hiroshi H Miyamoto Ryo R Komata Yosuke Y Kawamura Takeshi T Matsui Hirotaka H Inaba Toshiya T Takaori-Kondo Akifumi A Yokoyama Akihiko A

eLife 20210825

Leukemic oncoproteins cause uncontrolled self-renewal of hematopoietic progenitors by aberrant gene activation, eventually causing leukemia. However, the molecular mechanism underlying aberrant gene activation remains elusive. Here, we showed that leukemic MLL fusion proteins associate with the HBO1 histone acetyltransferase (HAT) complex through their trithorax homology domain 2 (THD2) in various human cell lines. MLL proteins associated with the HBO1 complex through multiple contacts mediated ...[more]

PMID: 34431785

Similar Datasets

Proteome analysis of affinity-purified protein co-precipitates

Project description:β-adrenergic signaling-regulated MYPT1-PP1β phosphatase bridges chromatin states and actomysin tension-mediated YAP/TAZ transcriptional network for beige adipogenesis

2022-09-28 | PXD031897 | JPOST Repository

Proteome analysis of affinity-purified protein co-precipitates

Project description:Proteome analysis of affinity-purified materials prepared from nucleosome/chromatin fractions of HEK293T cells expressing various constructs.

2020-09-26 | PXD015591 | JPOST Repository

Proteome analysis of affinity-purified protein co-precipitates

Project description:RNA-Binding Proteins Control the Oncogenic Activity of MLL-AF4

2022-04-19 | PXD025464 | JPOST Repository

Proteome analysis of affinity-purified protein co-precipitates

Project description:Spatiotemporal Dynamics of SETD5-containing NCoR- HDAC3 Complex Determines Enhancer Activation for Adipogenesis

2021-10-22 | PXD029279 | JPOST Repository

Proteome analysis of affinity-purified protein co-precipitates

Project description:Proteome analysis of affinity-purified materials prepared from chromatin fractions of HEK293T cells expressing various constructs. HEK293T cells transiently expressing various constructs were subjected to fanChIP (fractionation-assisted chromatin immunoprecipitation) method described in our previous paper (Okuda et al. 2014 Nucleic Acids Research 42;7 p4241-4256).

2021-06-15 | PXD019783 | JPOST Repository

Protein-protein interactions of tandem affinity purified protein kinases from rice.

Project description:Eighty-eight rice (Oryza sativa) cDNAs encoding rice leaf expressed protein kinases (PKs) were fused to a Tandem Affinity Purification tag (TAP-tag) and expressed in transgenic rice plants. The TAP-tagged PKs and interacting proteins were purified from the T1 progeny of the transgenic rice plants and identified by tandem mass spectrometry. Forty-five TAP-tagged PKs were recovered in this study and thirteen of these were found to interact with other rice proteins with a high probability score. In vivo phosphorylated sites were found for three of the PKs. A comparison of the TAP-tagged data from a combined analysis of 129 TAP-tagged rice protein kinases with a concurrent screen using yeast two hybrid methods identified an evolutionarily new rice protein that interacts with the well conserved cell division cycle 2 (CDC2) protein complex.

| S-EPMC2723914 | biostudies-literature

Proteome Profiling of Exosomes Purified from a Small Amount of Human Serum: The Problem of Co-Purified Serum Components.

Project description:Untargeted proteomics analysis of extracellular vesicles (EVs) isolated from human serum or plasma remains a technical challenge due to the contamination of these vesicles with lipoproteins and other abundant serum components. Here we aimed to test a simple method of EV isolation from a small amount of human serum (<1 mL) using the size-exclusion chromatography (SEC) standalone for the discovery of vesicle-specific proteins by the untargeted LC-MS/MS shotgun approach. We selected the SEC fraction containing vesicles with the size of about 100 nm and enriched with exosome markers CD63 and CD81 (but not CD9 and TSG101) and analyzed it in a parallel to the subsequent SEC fraction enriched in the lipoprotein vesicles. In general, there were 267 proteins identified by LC-MS/MS in exosome-containing fraction (after exclusion of immunoglobulins), yet 94 of them might be considered as serum proteins. Hence, 173 exosome-related proteins were analyzed, including 92 proteins absent in lipoprotein-enriched fraction. In this set of exosome-related proteins, there were 45 species associated with the GO cellular compartment term "extracellular exosome". Moreover, there were 31 proteins associated with different immune-related functions in this set, which putatively reflected the major role of exosomes released by immune cells present in the blood. We concluded that identified set of proteins included a bona fide exosomes components, yet the coverage of exosome proteome was low due to co-purified high abundant serum proteins. Nevertheless, the approach proposed in current work outperformed other comparable protocols regarding untargeted identification of exosome proteins and could be recommended for pilot exploratory studies when a small amount of a serum/plasma specimen is available.

| S-EPMC6630217 | biostudies-literature

Evaluation of affinity purified RNA-protein complexes related with NMD

Project description:Nonsense-mediated mRNA decay (NMD) is a conserved RNA degradation pathway that is involved in development, resistance to viral infections and evolution. Upf1, a core NMD factor, is associated with a large variety of cellular RNA in complex ribonucleoprotein particles. We characterized NMD complexes previously by affinity purification of tagged protein followed by mass spectrometry. Here, we extend our observations to proteins that are present in NMD complexes, but for whom the interaction with NMD factors is mediated by RNA. We purified tagged versions of Lsm1, Lsm7, Pat1, Dhh1 and Pab1 and assessed the presence and amount of NMD and RNA-related proteins in each purification. As expected from our previously published results, Upf1 was present in these purifications, suggesting novel hypotheses about the role of Pab1 and the Lsm1-7 complexes in RNA degradation.

2023-08-30 | PXD028008 | Pride

SKP2-affinity-purified mass spectrometry analysis.

Project description:This project aims to identify the SKP2 interaction proteins.

2023-01-05 | PXD039225 | Pride

Proteomic analysis of affinity-purified extracellular proteasomes reveals exclusively 20S complexes.

Project description:Proteasome-mediated proteolysis is important for many basic cellular processes. In addition to their functions in the cell, proteasomes have been found in physiological fluids of both healthy and diseased humans including cancer patients. Higher levels of these proteasomes are associated with higher cancer burden and stage. The etiology and functions of these proteasomes, referred to as circulating, plasmatic, or extracellular proteasomes (ex-PSs), are unclear. Here we show that human cancer cell lines, as well as human endometrium-derived mesenchymal stem cells (hMESCs), release proteasome complexes into culture medium (CM). To define ex-PS composition, we have affinity purified them from CM conditioned by human leukemia cell line K562. Using matrix-assisted laser desorption/ionization (MALDI) Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS), we have identified core 20S proteasome subunits and a set of 15 proteasome-interacting proteins (PIPs), all previously described as exosome cargo proteins. Three of them, PPIase A, aldolase A, and transferrin, have never been reported as PIPs. The study provides compelling arguments that ex-PSs do not contain 19S or PA200 regulatory particles and are represented exclusively by the 20S complex.

| S-EPMC5731941 | biostudies-literature

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