Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Human ZDHHC13 phosphorylation test

ABSTRACT: We use microcapillary LC/MS/MS to examine the phosphorylation sites of purified human ZDHHC13 protein.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Shuyang Chen

LAB HEAD: Shuyang Chen

PROVIDER: PXD038934 | Pride | 2023-10-24

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	37775_36255.mzXML	Mzxml
	37775_65750.mzid.gz	Mzid
	37775_out.tgz	Other
	37775_sequest.params	Other
	65750.mzXML	Mzxml

Items per page:

1 - 5 of 6

Publications

AMPK Phosphorylates ZDHHC13 to Increase MC1R Activity and Suppress Melanomagenesis.

Sun Yu Y Li Xin X Yin Chengqian C Zhang Judy J Liang Ershang E Wu Xianfang X Ni Ying Y Arbesman Joshua J Goding Colin R CR Chen Shuyang S

Cancer research 20230401 7

Inherited genetic variations in the melanocortin-1 receptor (MC1R) responsible for human red hair color (RHC) variants are associated with impaired DNA damage repair and increased melanoma risk. MC1R signaling is critically dependent on palmitoylation, primarily mediated by the protein acyltransferase zinc finger DHHC-type palmitoyltransferase 13 (ZDHHC13). A better understanding of how ZDHHC13 is physiologically activated could help identify approaches to prevent melanomagenesis in redheads. He ...[more]

PMID: 36701140

Similar Datasets

LC-MS of extracellular vesicles from Staphylococcus aureus USA300 JE2 and its agrspa double mutant strain

Project description:This project aims to identify the extracellular vesicles (EVs) from Staphylococcus aureus USA300 JE2 strain. In addition, we also detoxified the EVs by mutation of agr ad spa genes in JE2 and evaluated the immunogenicity and protection of the detoxified EVs. These proteins from these detoxified EVs were also identified by MS.

2018-10-23 | PXD007953 | Pride

The SAM domain-containing protein 1 (SAMD1) acts as a repressive chromatin regulator at unmethylated CpG islands

Project description:CpG-islands (CGIs) are key regulatory DNA elements at most promoters, but how they influence the chromatin status and transcription remains elusive. Here we identify and characterize SAMD1 (SAM domain-containing protein 1) as an unmethylated CGI-binding protein. SAMD1 possesses an atypical winged-helix domain that directly recognizes unmethylated CpG-containing DNA via simultaneous interactions with both the major and the minor groove. The SAM domain interacts with L3MBTL3, but it can also homopolymerize into a closed pentameric ring. At a genome-wide level, SAMD1 localizes to H3K4me3-decorated CGIs, where it acts as a repressor. SAMD1 tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs, thereby providing a mechanism for SAMD1-mediated transcriptional repression. Absence of SAMD1 impairs ES cell differentiation processes, leading to mis-regulation of key biological pathways. Together, our work establishes SAMD1 as a novel chromatin regulator acting at unmethylated CGIs.

2021-05-13 | PXD016781 | Pride

The interacted proteins of ALKBH5 and FTO identified by IP-mass

Project description:Since m6A demethylases (FTO and ALKBH5) have been reported to be involved in pre-mRNA splicing regulation, we hypothesized that dynamic m6A distribution during mRNA maturation might involve removal of m6A in internal exons by FTO or ALKBH5 accompanied by splicing factors. To explore this we performed pull-down assays coupled with protein mass spectrometry.

2022-12-09 | PXD038705 | Pride

The Mi-2 nucleosome remodeler and the Rpd3 histone deacetylase are involved in piRNA-guided heterochromatin formation

Project description:In eukaryotes, trimethylation of lysine 9 on histone H3 (H3K9) is associated with transcriptional silencing of transposable elements (TEs). In drosophila ovaries, this heterochromatic repressive mark is thought to be deposited by SetDB1 on TE genomic loci after the initial recognition of nascent transcripts by PIWI-interacting RNAs (piRNAs) loaded on the Piwi protein. Here, we show that the nucleosome remodeler Mi-2, in complex with its partner MEP-1, forms a subunit that is transiently associated, in a MEP-1 C-terminus-dependent manner, with known Piwi interactors, including a recently reported SUMO ligase Su(var)2-10. Together with the histone deacetylase Rpd3, this module is involved in the piRNA-dependent TE silencing, correlated with H3K9 deacetylation and trimethylation. Therefore. drosophila piRNA-mediated transcriptional silencing involves three epigenetic effectors, a remodeler, Mi-2, an eraser, Rpd3 and a writer, SetDB1, in addition to the Su(var)2-10 SUMO ligase.

2020-07-21 | PXD018749 | Pride

Identify proteins that interact with CDC25B

Project description:Identify proteins that interact with CDC25B in HS578T cells using Mass Spectrometry

2021-09-09 | PXD020368 | Pride

Truncated PARP1 promotes RNA Polymerase III during apoptosis

Project description:The N-terminal three zinc finger motifs of PARP1 are evolutionarily conserved in multicellular organism。However, during apoptosis, human PARP1 is mainly cleaved by caspase 3 at D214. As a result, the truncated PARP1 loses two N-terminal zinc finger motifs and only contains the third zinc finger motif, the BRCT domain, the WGR domain and the C-terminal catalytic domain. Interestingly, when we explored the domain architecture of PARP1 in other organisms, we found that similar to human tPARP1, PARP1 orthologs in several lower organisms do not have the N-terminal two zinc fingers or even they lack the third zinc finger motif. It indicates that even without the first two zinc finger motifs, tPARP1 may still catalyze ADP-ribosylation and play an important role in certain biological processes. To reveal the biological function of tPARP1, we performed tandem affinity purification and searched for the possible substrates.

2022-02-15 | PXD018691 | Pride

Protein compositions of extracellular vesicles released from Staphylococcus aurues JE2 and its lgt mutant

Project description:This project detected the protein composition of extracellular vesicles (EV) produced by S. aureus WT JE2 strain and its lgt mutant (lipoprotein deficient mutant). Our recent study found that mutation of lgt in S. aureus USA300 JE2 strain significantly increased EV production in S. aureus and decreased the pore-forming toxin content of vesicles, indicatiung that lipoproteins modulate the EV biogenesis of S. aureus. To gain a better understanding of this process, we detected the protein compositions associated with EVs purified from both WT and lgt mutant EVs by LC-MS/MS. Compared to WT EVs, more cytosoli proteins and less extracellular proteins were identified in lgt mutant EVs. A total of 180 and 198 proteins were identified from WT and lgt mutant EVs, respectively.In addition 27.2% and 33.8% of identified proteins were unique to WT or lgt mutant EVs respectively.

2021-09-08 | PXD014888 | Pride

In vivo BioID Mouse heart masspec data

Project description:Cardiac excitation-contraction (E-C) coupling requires dyads, the nanoscopic microdomains formed adjacent to Z-lines by apposition of transverse (T)-tubules and junctional sarcoplasmic reticulum (jSR). Disruption of dyad architecture and function are common features of diseased cardiomyocytes. However, little is known about the mechanisms that modulate dyad organization during cardiac homeostasis and disease. Here, we used proximity proteomics in intact, living hearts to identify proteins enriched near dyads.

2022-02-21 | PXD028960 | Pride

Expression data from knockdown of G9a in MDA-MB231 cells

Project description:G9a is an H3K9m2 methyltransferase, which is critical in controlling gene suppression and DNA methylation. We used microarray analysis to identify the target genes that are regulated by G9a in MDA-MB231 cells, in which E-cadherin is silenced. G9a expression was stably knocked-down in MDA-MB231 cells. RNA from this clone and parental (control) cells were purified for microarray analysis.

2012-01-07 | E-GEOD-34925 | biostudies-arrayexpress

OMA-1, LIN-41 IPMS - LIN-41 and OMA Ribonucleoprotein Complexes Mediate a Translational Repression-to-Activation Switch Controlling Oocyte Meiotic Maturation and the Oocyte-to-Embryo Transition in Caenorhabditis elegans

Project description:An extended meiotic prophase is a hallmark of oogenesis. Hormonal signaling activates the CDK1/cyclin B kinase to promote oocyte meiotic maturation, which involves nuclear and cytoplasmic events. Nuclear maturation encompasses nuclear envelope breakdown, meiotic spindle assembly, and chromosome segregation. Cytoplasmic maturation involves major changes in oocyte protein translation and cytoplasmic organelles and is poorly understood. In the nematode Caenorhabditis elegans, sperm release the major sperm protein (MSP) hormone to promote oocyte growth and meiotic maturation. Large translational regulatory ribonucleoprotein (RNP) complexes containing the RNA-binding proteins OMA-1, OMA-2, and LIN-41 regulate meiotic maturation downstream of MSP signaling. To understand the control of translation during meiotic maturation, we purified LIN-41-containing RNPs and characterized their protein and RNA components. Protein constituents of LIN-41 RNPs include essential RNA-binding proteins, the GLD-2 cytoplasmic poly(A) polymerase, the CCR4-NOT deadenylase complex, and translation initiation factors. RNA sequencing defined mRNAs associated with both LIN-41 and OMA-1, as well as sets of mRNAs associated with either LIN-41 or OMA-1. Genetic and genomic evidence suggests that GLD-2, which is a component of LIN-41 RNPs, stimulates the efficient translation of many LIN-41-associated transcripts. We analyzed the translational regulation of two transcripts specifically associated with LIN-41 that encode the RNA regulators SPN-4 and MEG-1. We found that LIN-41 represses translation of spn-4 and meg-1, whereas OMA-1 and OMA-2 promote their expression. Upon their synthesis, SPN-4 and MEG-1 assemble into LIN-41 RNPs prior to their functions in the embryo. This study defines a translational repression-to-activation switch as a key element of cytoplasmic maturation.

2017-06-16 | PXD006726 | 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