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. 2018 Dec 17;6(4):53. doi: 10.3390/proteomes6040053

Table 2.

Spinophilin interacting proteins that had altered abundance following amphetamine treatment.

Description # PSMs Normalized Abundance Ratio (Treatment)/(Control) Normalized Abundance Ratio (log2): (Treatment)/(Control)
Decreased Interactions
E3 ubiquitin-protein ligase XIAP 22 0.69 −0.54
Disks large homolog 3 143 0.67 −0.58
Granulins 10 0.36 −1.47
Increased Interactions
Myelin proteolipid protein 38 2.28 1.19
Hemoglobin subunit alpha 17 2.24 1.16
ADP/ATP translocase 2 36 2.23 1.16
Clathrin light chain A 17 2.13 1.09
Adenylyl cyclase-associated protein 2 8 2.10 1.07
MCG10343, isoform CRA_b 35 2.08 1.05
Tubulin alpha-1B chain 54 2.07 1.05
Tubulin alpha chain (Fragment) 54 2.03 1.02
Cytochrome c oxidase subunit NDUFA4 13 2.03 1.02
Profilin-2 14 2.02 1.02
Reticulon (Fragment) 20 2.02 1.01
Myelin-oligodendrocyte glycoprotein 18 2.01 1.01
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform 28 2.00 1.00

HA spinophilin was immunoprecipitated from saline and amphetamine-treated D1 Cre and A2A Cre mice. The abundance of the individual proteins was normalized to the abundance of spinophilin. A ratio of the abundance of proteins isolated from the amphetamine treated over the saline treated mice was generated. A subset of spinophilin interacting proteins that had at least eight spectral counts (PSMs) and had a decreased (<0.05) or increased (≥1.00) log2 ratio is shown. A complete list of interacting proteins (without contaminants) and their abundance ratios are shown in Table S2A.