| UniProt ID | IMPCT_MOUSE | |
|---|---|---|
| UniProt AC | O55091 | |
| Protein Name | Protein IMPACT | |
| Gene Name | Impact | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 318 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. [PubMed: 15937339] | |
| Protein Sequence | MAEEEVGNSQRQSEEIEAMAAIYGEEWCVIDENAKIFCIRVTDFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIYVHNMGESILYQWVEKIRDALIQKSQITEPDPDVKKKTEEVEVESEEDPILEHPPENPVKTLDLKISEETQPETEELPPVAHGVPITDRRSTFQAHVAPVVCPEQVKLVLAKLYENKKIASATHNIYAYRIFCEDKQTFLQDCEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNFTNTPDESTKNLGKKKVKKDKKKNDH | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 9 | Phosphorylation | AEEEVGNSQRQSEEI CHHHCCCCHHHHHHH | 22.32 | 22006019 | |
| 38 | S-nitrosocysteine | DENAKIFCIRVTDFM ECCCCEEEEEECCCC | 1.90 | - | |
| 38 | S-nitrosylation | DENAKIFCIRVTDFM ECCCCEEEEEECCCC | 1.90 | 21278135 | |
| 98 | Ubiquitination | EIYVHNMGESILYQW EEEHHCCCHHHHHHH | 30.71 | 27667366 | |
| 116 | Ubiquitination | IRDALIQKSQITEPD HHHHHHHHHHCCCCC | 37.02 | 27667366 | |
| 130 | Phosphorylation | DPDVKKKTEEVEVES CCCHHHHCEEEEECC | 46.38 | 24925903 | |
| 137 | Phosphorylation | TEEVEVESEEDPILE CEEEEECCCCCCCCC | 52.00 | 24925903 | |
| 159 | Phosphorylation | KTLDLKISEETQPET CEEEEEECCCCCCCC | 28.00 | 25338131 | |
| 204 | Ubiquitination | QVKLVLAKLYENKKI HHHHHHHHHHCCCCH | 47.65 | 22790023 | |
| 206 | Phosphorylation | KLVLAKLYENKKIAS HHHHHHHHCCCCHHH | 19.42 | 20139300 | |
| 210 | Ubiquitination | AKLYENKKIASATHN HHHHCCCCHHHCCCC | 55.90 | 22790023 | |
| 213 | Phosphorylation | YENKKIASATHNIYA HCCCCHHHCCCCEEE | 36.85 | 20139300 | |
| 215 | Phosphorylation | NKKIASATHNIYAYR CCCHHHCCCCEEEEE | 16.98 | 20139300 | |
| 219 | Phosphorylation | ASATHNIYAYRIFCE HHCCCCEEEEEEEEC | 11.69 | 20139300 | |
| 221 | Phosphorylation | ATHNIYAYRIFCEDK CCCCEEEEEEEECCH | 6.30 | 20139300 | |
| 228 | Ubiquitination | YRIFCEDKQTFLQDC EEEEECCHHHEECCC | 29.01 | 22790023 | |
| 284 | Ubiquitination | FKHINNCARNILVEK HHHHHHHHHHHHEEC | 15.07 | 27667366 | |
| 291 | Ubiquitination | ARNILVEKNFTNTPD HHHHHEECCCCCCCC | 50.29 | 22790023 | |
| 296 | Phosphorylation | VEKNFTNTPDESTKN EECCCCCCCCHHHHC | 29.11 | 25521595 | |
| 302 | Ubiquitination | NTPDESTKNLGKKKV CCCCHHHHCCCCHHC | 60.50 | 27667366 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of IMPCT_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IMPCT_MOUSE !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of IMPCT_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CDK1_YEAST | CDC28 | physical | 26176233 | |
| CDK1_MOUSE | Cdk1 | physical | 26176233 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASSSPECTROMETRY. | |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASSSPECTROMETRY. | |
| "Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASSSPECTROMETRY. | |