INT339845

Context Info Confidence 0.23 First Reported 2010 Last Reported 2010 Negated 0 Speculated 0 Reported most in Body Documents 1 Total Number 4 Disease Relevance 0.31 Pain Relevance 0.20

cell proliferation (UCN2) extracellular space (UCN2) extracellular region (UCN2) response to stress (UCN2)

UCN2 (Homo sapiens)

Pain Link Frequency Relevance Heat imagery 4 77.76 Inflammation 24 70.56 tolerance 28 5.00 rheumatoid arthritis 12 5.00 cytokine 8 5.00 Sicca syndrome 8 5.00 Osteoarthritis 8 5.00 Inflammatory mediators 4 5.00 IPN 4 5.00 Arthritis 4 5.00

Disease Link Frequency Relevance Heat INFLAMMATION 20 70.56 Myositis 4 55.68 Dermatomyositis 36 41.68 Apoptosis 32 25.72 Rheumatic Diseases 20 5.00 Rheumatoid Arthritis 12 5.00 Arthritis 8 5.00 Systemic Lupus Erythematosus 8 5.00 Autoimmune Disease 8 5.00 Syndrome 8 5.00

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Anatomy

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-stimulated Jurkat cells were evaluated by WB using antibodies against SRP72, SRP54 (nonphosphorylated form of SRP), and GAPDH (loading control).

Phosphorylation (nonphosphorylated) of SRP

1) Confidence 0.23 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0

g/ml) to human SRP72 epitope mapping near the C terminus of SRP72 of human origin (Santa Cruz Biotechnology, 1:2500), human SRP54 (Sigma) (1:2500), which represents the nonphosphorylated SRP protein and human GAPDH (Syd Labs, Boston) (1:3000).

Phosphorylation (nonphosphorylated) of SRP

2) Confidence 0.22 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0 Pain Relevance 0.04

We suggest a few possible applications of this reaction on the cell physiology as follows. 1) It has been described that a GTPase domain on the docking protein for SRP at the rough ER could be related to the release of the complex SRP-docking-ribosome-mRNA-translocon (5, 24, 26–28). 2) The phosphorylation of the SRP72 might increase the affinity of SRP for its receptor on the rough ER membrane and facilitate the rough ER translocation of protein (5, 23, 29–31). 3) The phosphorylation of SRP72 influence on the SRP complex activity in general because of the targeting of the protein by SRP does not requires GTPase activity (31–35).

Phosphorylation (phosphorylation) of SRP

3) Confidence 0.17 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.14 Pain Relevance 0.07

We suggest a few possible applications of this reaction on the cell physiology as follows. 1) It has been described that a GTPase domain on the docking protein for SRP at the rough ER could be related to the release of the complex SRP-docking-ribosome-mRNA-translocon (5, 24, 26–28). 2) The phosphorylation of the SRP72 might increase the affinity of SRP for its receptor on the rough ER membrane and facilitate the rough ER translocation of protein (5, 23, 29–31). 3) The phosphorylation of SRP72 influence on the SRP complex activity in general because of the targeting of the protein by SRP does not requires GTPase activity (31–35).

Phosphorylation (phosphorylation) of SRP

4) Confidence 0.17 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2963399 Disease Relevance 0.18 Pain Relevance 0.09

General Comments

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