IMPCT_MOUSE - dbPTM
IMPCT_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
9PhosphorylationAEEEVGNSQRQSEEI
CHHHCCCCHHHHHHH
22.3222006019
38S-nitrosocysteineDENAKIFCIRVTDFM
ECCCCEEEEEECCCC
1.90-
38S-nitrosylationDENAKIFCIRVTDFM
ECCCCEEEEEECCCC
1.9021278135
98UbiquitinationEIYVHNMGESILYQW
EEEHHCCCHHHHHHH
30.7127667366
116UbiquitinationIRDALIQKSQITEPD
HHHHHHHHHHCCCCC
37.0227667366
130PhosphorylationDPDVKKKTEEVEVES
CCCHHHHCEEEEECC
46.3824925903
137PhosphorylationTEEVEVESEEDPILE
CEEEEECCCCCCCCC
52.0024925903
159PhosphorylationKTLDLKISEETQPET
CEEEEEECCCCCCCC
28.0025338131
204UbiquitinationQVKLVLAKLYENKKI
HHHHHHHHHHCCCCH
47.6522790023
206PhosphorylationKLVLAKLYENKKIAS
HHHHHHHHCCCCHHH
19.4220139300
210UbiquitinationAKLYENKKIASATHN
HHHHCCCCHHHCCCC
55.9022790023
213PhosphorylationYENKKIASATHNIYA
HCCCCHHHCCCCEEE
36.8520139300
215PhosphorylationNKKIASATHNIYAYR
CCCHHHCCCCEEEEE
16.9820139300
219PhosphorylationASATHNIYAYRIFCE
HHCCCCEEEEEEEEC
11.6920139300
221PhosphorylationATHNIYAYRIFCEDK
CCCCEEEEEEEECCH
6.3020139300
228UbiquitinationYRIFCEDKQTFLQDC
EEEEECCHHHEECCC
29.0122790023
284UbiquitinationFKHINNCARNILVEK
HHHHHHHHHHHHEEC
15.0727667366
291UbiquitinationARNILVEKNFTNTPD
HHHHHEECCCCCCCC
50.2922790023
296PhosphorylationVEKNFTNTPDESTKN
EECCCCCCCCHHHHC
29.1125521595
302UbiquitinationNTPDESTKNLGKKKV
CCCCHHHHCCCCHHC
60.5027667366

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMPCT_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDK1_YEASTCDC28physical
26176233
CDK1_MOUSECdk1physical
26176233

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IMPCT_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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