Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Identification of phosphorylated amino acids in CgSub2 protein in Candida glabrata

ABSTRACT: The objective of the project is to identify the phosphorylated amino acid residues in CgSub2 in the pathogenic yeast Candida glabrata. For this analysis, wild-type cells and mutants lacking CgHog1 MAPK or CgSlt2MAPK or both CgHog1 and CgSlt2 MAPKs were used.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Candida Glabrata (yeast) (torulopsis Glabrata)

SUBMITTER: Rupinder Kaur

LAB HEAD: Rupinder Kaur

PROVIDER: PXD049381 | Pride | 2024-05-06

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	56911_out.tgz	Other
	56912_out.tgz	Other
	56913_out.tgz	Other
	56914_out.tgz	Other
	79565.raw	Raw

Items per page:

1 - 5 of 9

Similar Datasets

CgSub2 interactome analysis in the presence and absence of CgHog1 MAPK in Candida glabrata

Project description:The objective of the project is to identify CgSub2-interacting proteins in the presence and absence of CgHog1 MAPK in the pathogenic yeast Candida glabrata, with CgSub2 being an interactor of CgHog1.

2024-05-06 | PXD049223 | Pride

Interactome analysis of the CgHog1 MAPK under varied-iron conditions in Candida glabrata

Project description:The objective of the project is to identify proteins that interact with CgHog1 under low-iron, regular-iron and high-iron growth conditions in the pathogenic yeast Candida glabrata.

2024-05-06 | PXD049380 | Pride

Interactome identification of Histones H3 and H4 in the presence and absence of methyl methanesulfonate (MMS) in the pathogenic yeast Candida glabrata

Project description:The main goal of this project is to identify proteins in Candida glabrata that interact with histones H3 (CgHht) and H4 (CgHhf) under normal and MMS-treatment conditions.

2020-02-21 | PXD016867 | Pride

Interactome identification of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the pathogenic yeast Candida glabrata

Project description:The major goal of this project is to identify proteins that interact with CgYps1 aspartyl protease in logarithmic-phase Candida glabrata cells.

2021-02-08 | PXD022766 | Pride

Phosphatidylinositol 3-phosphate (PI3P) interactome analysis under varied iron conditions in Candida glabrata.

Project description:The project is aimed at identifying proteins that interact with PI3P in low-iron, regular-iron and high-iron grown Candida glabrata cells.

2024-02-19 | PXD042058 | Pride

HOXB13 WT and G84E mass spectrometry

Project description:To identify potential cofactors of HOXB13 in suppressing lipogenic programs in prostate cancer cells, we performed tandem affinity purification followed by mass spectrometry analysis of WT and G84E HOXB13 expressed in LNCaP cells. Out of the HOXB13-enriched proteins are previously reported interactors such as AR and its cofactors FOXA1, GATA2, and NKX3. However, these interactions were not disrupted by G84E as compared to WT HOXB13. Interestingly, we found strong interactions of HOXB13 with HDAC1/3 and their corepressors NCoR1/2 and TBL1X. Notably, these interactions were drastically reduced by G84E mutation.

2023-03-11 | PXD030810 | Pride

SFB-tagged(S-protein tag, Flag epitope tag, and streptavidin-binding peptide tag) RNF4 wild-type and CS mutant LC-MSMS

Project description:To elucidate the role of RNF4 in DNA replication and fork reversal, we performed tandem affinity purification (TAP) using a HEK293T cell line that stably expresses SFB-tagged(S-protein tag, Flag epitope tag, and streptavidin-binding peptide tag) wild-type and CS mutant to isolate proteins that associate with RNF4.

2022-08-11 | PXD028397 | Pride

ASF1 acts with RIF1 to promote DNA end-joining in BRCA1 deficient cells

Project description:RIF1 acts downstream of 53BP1 to coordinate DNA double strand break repair pathway choice between non-homologous end joining (NHEJ) and homologous recombination (HR). Here we identified ASF1 as an endogenous RIF1-associated protein. We showed that ASF1 forms complex with RIF1 and regulates RIF1-dependent functions in DNA damage response.

2022-06-09 | PXD027727 | Pride

Quantitative RNA interactome capture (qRIC) identifies phosphorylation sites with regulatory potential - RBM20 BioID

Project description:RNA binding proteins (RBPs) are major regulators of gene expression at the post-transcriptional level. While many posttranslational modification sites in RBPs have been identified, less is known about how these modifications regulate RBP function. Here, we develop quantitative RNA-interactome capture (qRIC) to quantify the fraction of cellular RBPs pulled down with polyadenylated mRNAs. Applying qRIC to HEK293T cells quantified pulldown efficiencies of over 300 mRBPs. Combining qRIC with phosphoproteomics allowed us to systematically compare pulldown efficiencies of phosphorylated and non-phosphorylated forms of mRBPs. Over hundred phosphorylation sites show increased or decreased pull-down efficiency compared to their host RBPs and thus have regulatory potential. Our data captures known regulatory phosphorylation sites in ELAVL1, SF3B1 and UPF1 and identifies new potentially regulatory sites. Follow-up experiments on the cardiac splicing regulator RBM20 revealed that multiple phosphorylation sites in the C-terminal disordered region affect nucleo-cytoplasmic shuttling, association with cytosolic RNA granules and alternative splicing. Together, we show that qRIC is a scalable method to identify the function of posttranslational modifications in RBPs.

2022-09-05 | PXD027138 | Pride

CTCF cooperates with CtIP to drive homologous recombination repair of double-strand breaks

Project description:The pleiotropic CCCTC-binding factor (CTCF) plays a role in homologous recombination (HR) repair of DNA double-strand breaks (DSBs). However, the precise mechanistic role of CTCF in HR remains largely unclear. Here, we show that CTCF engages in DNA end resection, which is the initial, crucial step in HR, through its interactions with MRE11 and CtIP. Depletion of CTCF profoundly impairs HR and attenuates CtIP recruitment at DSBs. CTCF physically interacts with MRE11 and CtIP and promotes CtIP recruitment to sites of DNA damage. Subsequently, CTCF facilitates DNA end resection to allow HR, in conjunction with MRE11-CtIP. Notably, the zinc finger domain of CTCF binds to both MRE11 and CtIP and enables proficient CtIP recruitment, DNA end resection, and HR. The N-terminus of CTCF is able to bind to only MRE11 and its C-terminus is incapable of binding to MRE11 and CtIP, thereby resulting in compromised CtIP recruitment, DSB resection, and HR. Overall, this suggests an important function of CTCF in DNA end resection through the recruitment of CtIP at DSBs. Collectively, our findings identify a critical role of CTCF at the first control point in selecting the HR repair pathway

2019-11-12 | PXD014441 | 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