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UnknownSignal peptide peptidase-like 2c impairs vesicular transport and cleaves SNARE proteins.
Not available
S-EPMC6399617 | biostudies-literature
UnknownSignal Peptide-Peptidase-Like 2c (SPPL2c) impairs vesicular transport and cleavage of SNARE proteins
Not available
S-SCDT-EMBOR-2018-46451-T | biostudies-other
ProteomicsQuantitative Proteomics of SPPL2c overexpressing HEK cells
Signal peptide peptidase-like 2c (SPPL2c) is the only member of the GxGD type intramembrane-cleaving aspartyl proteases that so far has not been assigned any substrates and thus its capability of proteolysis and its physiological function remain enigmatic. Based on a surprisingly high expression of ...
ORGANISM(S): Homo sapiens (Human) 
2019-02-12 | PXD011923 | Pride
Sppl2c Hek cells 
ProteomicsSelective regulation of aspartyl intramembrane protease activity by calnexin
Signal peptide peptidase-like 2c (SPPL2c) is a testis-specific aspartyl intramembrane protease that contributes to male gamete function both by catalytic and non-proteolytic mechanisms. Here, we provide an unbiased characterisation of the in vivo interactome of SPPL2c identifying the ER chaperone ca...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-07 | PXD052965 | Pride
Co-ip Signal peptide peptidase-like 2c Mouse Calnexin Sppl2c Testis 
ProteomicsIdentification of phosphorylation sites regulated by lysophosphatidic acid (LPA) in OVCAR8 ovarian cancer cells
Elevated levels of lysophosphatidic acid (LPA) species accumulate in the ascites of ovarian high grade serous cancer (HGSC) and are associated with a short relapse-free survival. LPA is known to support the metastatic spread of cancer cells by activating a multitude of signaling pathways through G-p...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-01-26 | MSV000091158 | MassIVE
ProteomicsIdentification of phosphorylation sites regulated by lysophosphatidic acid (LPA) in OCMI91s ovarian cancer cells
Elevated levels of lysophosphatidic acid (LPA) species accumulate in the ascites of ovarian high grade serous cancer (HGSC) and are associated with a short relapse-free survival. LPA is known to support the metastatic spread of cancer cells by activating a multitude of signaling pathways through G-p...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-01-25 | MSV000091146 | MassIVE
ProteomicsPeroxisomal targeting of the protein phosphatase Ptc5 via mitochondrial transit
Correct intracellular distribution of proteins is critical for the function of eukaryotic cells. Certain proteins are targeted to more than one cellular compartment, e.g. to mitochondria and peroxisomes. The protein phosphatase Ptc5 from Saccharomyces cerevisiae contains an N-terminal mitochondrial ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-05-22 | PXD018591 | Pride
Protein phosphatase Yeast Peroxisome Ptc5 
UnknownThe transmembrane domain of Frey1 harbors a transplantable inhibitory motif for intramembrane proteases.
Not available
S-EPMC10234869 | biostudies-literature
GenomicsUsp_W3L
modENCODE_submission_4109 This submission comes from a modENCODE project of Kevin White. For full list of modENCODE projects, see http://www.genome.gov/26524648 Project Goal: The White Lab is aiming to map the association of all the Transcription Factors (TF) on the genome of Drosophila melanogaster...
ORGANISM(S): Drosophila melanogaster 
2013-08-28 | E-GEOD-50358 | biostudies-arrayexpress
GenomicsUSP-GFP_WPP+12-seq
modENCODE_submission_4113 This submission comes from a modENCODE project of Kevin White. For full list of modENCODE projects, see http://www.genome.gov/26524648 Project Goal: The White Lab is aiming to map the association of all the Transcription Factors (TF) on the genome of Drosophila melanogaster...
ORGANISM(S): Drosophila melanogaster 
2013-08-28 | E-GEOD-50359 | biostudies-arrayexpress
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