PXD000834 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Positional proteomics identification of the natural substrates of cytosolic carboxypeptidases |
Description | Cytosolic carboxypeptidases (CCPs) constitute a new subfamily of M14 metallocarboxypeptidases associated to axonal regeneration and neuronal degeneration, amongst others. CCPs are deglutamylating enzymes, able to catalyze the shortening of polyglutamate side-chains and the gene-encoded C-termini of tubulin, telokin and myosin light chain kinase. The functions of these enzymes are not entirely understood, in part due to lack of information about C-terminal protein processing in the cell and its functional implications. By means of C-terminal COFRADIC, a positional proteomics approach, we searched for cellular substrates targets of CCP1, the most relevant member of this family. We here identified 7 new putative CCP1 protein substrates, including ribosomal proteins, translation factors and high mobility group proteins. |
HostingRepository | PRIDE |
AnnounceDate | 2014-12-02 |
AnnouncementXML | Submission_2014-12-02_04:56:56.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD000834 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Sebastian Tanco |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | 4x(2)H labeled alpha-dimethylamino N-terminal residue: 32.056407; 2-pyrrolidone-5-carboxylic acid (Gln): -17.026549; 3x(2)H labeled N6-acetyl-L-lysine: 45.029395; N-acetylated residue: 42.010565; L-methionine (S)-sulfoxide: 15.994915; acetate labeling reagent (N-term) (heavy form: +3amu) |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2014-03-17 03:28:15 | ID requested | |
⏵ 1 | 2014-12-02 04:56:57 | announced | |
Publication List
Tanco S, Tort O, Demol H, Aviles FX, Gevaert K, Van Damme P, Lorenzo J, C-terminomics screen for natural substrates of cytosolic carboxypeptidase 1 reveals processing of acidic protein C termini. Mol Cell Proteomics, 14(1):177-90(2015) [pubmed] |
Keyword List
ProteomeXchange project tag: PRIME-XS Project |
curator keyword: Biological |
submitter keyword: degradomics C-terminomics carboxypeptidase |
Contact List
Kris Gevaert |
contact affiliation | VIB Department of Medical Protein Research, UGent Proteome Analysis and Bioinformatics Unit B9000 Gent, Belgium |
contact email | Kris.Gevaert@vib-ugent.be |
lab head | |
Sebastian Tanco |
contact affiliation | Department of Medical Protein Research, VIB-Ghent University |
contact email | sebastian.tanco@vib-ugent.be |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD000834
- Label: PRIDE project
- Name: Positional proteomics identification of the natural substrates of cytosolic carboxypeptidases