PXD002228

PXD002228 is an original dataset announced via ProteomeXchange.

Title	Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and S250 phosphorylation in the conserved C-terminal regions
Description	The function of mammalian Bcnt protein is poorly understood yet, though Bcnt homologs (yeast Swc5 and Dorsophila Yeti) play crucial roles in chromatin remodeling organization. In this study, we found that mammalian Bcnt protein shows unusual mobility on SDS-PAGE and is acetylated in vitro by CREB-binding protein. Therefore, we analyzed Bcnt protein by LC-MSMS to characterize the protein structure containing post-translational modifications (phosphorylation and acetylation) which may be the cause of this unusual mobility.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:24:12.433.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Takehiro Suzuki
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	S-carboxamidoethyl-L-cysteine; phosphorylated residue; acetylated residue; monohydroxylated residue; deamidated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2015-05-26 03:06:11	ID requested
1	2015-06-25 03:57:40	announced
⏵ 2	2024-10-22 04:24:12	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

curator keyword: Biological, Biomedical

submitter keyword: Q Exactive,Homo sapiens

Takehiro Suzuki
contact affiliation	Biomolecular characterization unit, Center for Sustainable Resource Science, RIKEN
contact email	takehirosuzuki@riken.jp
lab head
Takehiro Suzuki
contact affiliation	RIKEN Center for Sustainable Resource Science
contact email	takehirosuzuki@riken.jp
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002228
     1. Label: PRIDE project
     2. Name: Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and S250 phosphorylation in the conserved C-terminal regions