Table 1.

Top 10 increased proteins in lysates of resting ERp5 knockout platelets

ProteinNameLog FCAverage expressionPAdjusted PFunctionIntracellular location
Nucb2 Nucleobindin-2 2.0 27.6 .0002 Ca2+ binding ER cytoplasm 
Hspa5 78 kilodalton glucose-regulated protein 1.2 34.8 .0002 ER chaperone ER 
Dnajc3 DnaJ homolog subfamily C member 3 1.5 29.7 .0004 Unfolded protein response, inhibition of phosphorylation of eIF2a ER 
Hsp90b1 Endoplasmin 1.0 34.1 .0004 ER chaperone, transport of secreted proteins ER 
Pdia4 (ERp72) Protein disulfide isomerase A4 1.2 31.4 .0005 Disulfide isomerase ER 
Hyou1 Hypoxia upregulated protein 1 1.0 31.7 .0013 Hypoxia upregulated, ER stress ER 
Pdia3 (ERp57) Protein disulfide isomerase A3 0.8 34.3 .0016 Disulfide isomerase ER 
Manf Mesencephalic astrocyte–derived neurotrophic factor 1.1 30.9 .0057 Hypoxia upregulated, ER stress ER 
Copg1 Coatomer subunit gamma-1 0.9 28.4 .0063 Protein transport from the ER to Golgi vesicles Cytoplasm 
10 Sdf2l1 Stromal cell-derived factor 2-like protein 1 1.2 29.2 .0066 Chaperone cofactor ER 
ProteinNameLog FCAverage expressionPAdjusted PFunctionIntracellular location
Nucb2 Nucleobindin-2 2.0 27.6 .0002 Ca2+ binding ER cytoplasm 
Hspa5 78 kilodalton glucose-regulated protein 1.2 34.8 .0002 ER chaperone ER 
Dnajc3 DnaJ homolog subfamily C member 3 1.5 29.7 .0004 Unfolded protein response, inhibition of phosphorylation of eIF2a ER 
Hsp90b1 Endoplasmin 1.0 34.1 .0004 ER chaperone, transport of secreted proteins ER 
Pdia4 (ERp72) Protein disulfide isomerase A4 1.2 31.4 .0005 Disulfide isomerase ER 
Hyou1 Hypoxia upregulated protein 1 1.0 31.7 .0013 Hypoxia upregulated, ER stress ER 
Pdia3 (ERp57) Protein disulfide isomerase A3 0.8 34.3 .0016 Disulfide isomerase ER 
Manf Mesencephalic astrocyte–derived neurotrophic factor 1.1 30.9 .0057 Hypoxia upregulated, ER stress ER 
Copg1 Coatomer subunit gamma-1 0.9 28.4 .0063 Protein transport from the ER to Golgi vesicles Cytoplasm 
10 Sdf2l1 Stromal cell-derived factor 2-like protein 1 1.2 29.2 .0066 Chaperone cofactor ER 

Protein function data have been sourced from UniProt.

Log FC, log fold change.

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