UniProt ID | HEK2_YEAST | |
---|---|---|
UniProt AC | P38199 | |
Protein Name | Heterogeneous nuclear rnp K-like protein 2 | |
Gene Name | HEK2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 381 | |
Subcellular Localization | Cytoplasm. Cytoplasm, P-body. Nucleus. Chromosome, telomere. | |
Protein Description | RNA-binding protein involved in the correct localization of transcripts in the cell. RNA localization is a widespread mechanism for achieving localized protein synthesis. Required for the asymmetric localization to the daughter cell nucleus of the ASH1 transcript, coding for a specific repressor of transcription. Overexpression inhibits translation of the ASH1 transcript. Involved in the stability of transcripts such as the MTL1 mRNA. Involved in structural and functional organization of telomeric chromatin and regulates silencing at the HMR locus.. | |
Protein Sequence | MSQFFEAATPVAIPTNNTNGGSSDAGSAATGGAPVVGTTAQPTINHRLLLSLKEAAKIIGTKGSTISRIRAANAVKIGISEKVPGCSDRILSCAGNVINVANAIGDIVDVLNKRNPENEDAAEGEAEEHYYFHFLNHILPAPSKDEIRDLQQLEDIGYVRLIVANSHISSIIGKAGATIKSLINKHGVKIVASKDFLPASDERIIEIQGFPGSITNVLIEISEIILSDVDVRFSTERSYFPHLKKSSGEPTSPSTSSNTRIELKIPELYVGAIIGRGMNRIKNLKTFTKTNIVVERKDDDDKDENFRKFIITSKFPKNVKLAESMLLKNLNTEIEKRENYKRKLEAAEGDATVVTERSDSASFLEEKEEPQENHDNKEEQS | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSQFFEAAT ------CCHHHHHCC | 35.38 | 24909858 | |
15 | Phosphorylation | ATPVAIPTNNTNGGS CCCEEECCCCCCCCC | 34.68 | 30377154 | |
18 | Phosphorylation | VAIPTNNTNGGSSDA EEECCCCCCCCCCCC | 36.99 | 30377154 | |
82 | Acetylation | VKIGISEKVPGCSDR EEEECCCCCCCCCHH | 47.11 | 24489116 | |
194 | Succinylation | GVKIVASKDFLPASD CCEEEECCCCCCCCC | 42.64 | 23954790 | |
194 | Acetylation | GVKIVASKDFLPASD CCEEEECCCCCCCCC | 42.64 | 24489116 | |
246 | Phosphorylation | YFPHLKKSSGEPTSP HCCCCCCCCCCCCCC | 41.82 | 22890988 | |
247 | Phosphorylation | FPHLKKSSGEPTSPS CCCCCCCCCCCCCCC | 56.93 | 22890988 | |
251 | Phosphorylation | KKSSGEPTSPSTSSN CCCCCCCCCCCCCCC | 49.30 | 22890988 | |
252 | Phosphorylation | KSSGEPTSPSTSSNT CCCCCCCCCCCCCCC | 27.80 | 25521595 | |
254 | Phosphorylation | SGEPTSPSTSSNTRI CCCCCCCCCCCCCCE | 40.46 | 22890988 | |
255 | Phosphorylation | GEPTSPSTSSNTRIE CCCCCCCCCCCCCEE | 39.29 | 22890988 | |
256 | Phosphorylation | EPTSPSTSSNTRIEL CCCCCCCCCCCCEEE | 26.40 | 22890988 | |
257 | Phosphorylation | PTSPSTSSNTRIELK CCCCCCCCCCCEEEE | 42.16 | 22890988 | |
259 | Phosphorylation | SPSTSSNTRIELKIP CCCCCCCCCEEEECC | 34.66 | 22890988 | |
289 | Acetylation | KNLKTFTKTNIVVER CCCCCCCCCCEEEEE | 35.07 | 24489116 | |
314 | Acetylation | RKFIITSKFPKNVKL HHHHHHCCCCCCCHH | 57.97 | 24489116 | |
320 | Acetylation | SKFPKNVKLAESMLL CCCCCCCHHHHHHHH | 51.91 | 24489116 | |
324 | Phosphorylation | KNVKLAESMLLKNLN CCCHHHHHHHHHHHC | 14.77 | 30377154 | |
328 | Acetylation | LAESMLLKNLNTEIE HHHHHHHHHHCHHHH | 56.26 | 24489116 | |
343 | Ubiquitination | KRENYKRKLEAAEGD HHHHHHHHHHHHCCC | 46.67 | 23749301 | |
352 | Phosphorylation | EAAEGDATVVTERSD HHHCCCCEEEEECCC | 21.90 | 29136822 | |
355 | Phosphorylation | EGDATVVTERSDSAS CCCCEEEEECCCCCH | 22.73 | 29136822 | |
358 | Phosphorylation | ATVVTERSDSASFLE CEEEEECCCCCHHHH | 29.68 | 19823750 | |
360 | Phosphorylation | VVTERSDSASFLEEK EEEECCCCCHHHHHC | 27.36 | 17330950 | |
362 | Phosphorylation | TERSDSASFLEEKEE EECCCCCHHHHHCCC | 34.02 | 22369663 | |
367 | Acetylation | SASFLEEKEEPQENH CCHHHHHCCCCCCCC | 58.98 | 24489116 | |
377 | Acetylation | PQENHDNKEEQS--- CCCCCCCHHHCC--- | 69.55 | 24489116 | |
381 | Phosphorylation | HDNKEEQS------- CCCHHHCC------- | 45.53 | 22890988 |
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 HEK2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HEK2_YEAST !! |
* 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 HEK2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; SER-358; SER-360;SER-362 AND SER-381, AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; SER-360 ANDSER-362, AND MASS SPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND MASSSPECTROMETRY. |