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 | ||
* 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 | ||||||
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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. |