| UniProt ID | ENP1_YEAST | |
|---|---|---|
| UniProt AC | P38333 | |
| Protein Name | Essential nuclear protein 1 | |
| Gene Name | ENP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 483 | |
| Subcellular Localization | Cytoplasm. Nucleus, nucleolus. | |
| Protein Description | Required for normal export of the pre-40S particles from the nucleus to the cytoplasm. Its subcellular location and association with pre-40S subunit shifts from mixed cytoplasm/nucleus to all nuclear in RPS19 disruptions, suggesting it acts after the ribosomal protein.. | |
| Protein Sequence | MARASSTKARKQRHDPLLKDLDAAQGTLKKINKKKLAQNDAANHDAANEEDGYIDSKASRKILQLAKEQQDEIEGEELAESERNKQFEARFTTMSYDDEDEDEDEDEEAFGEDISDFEPEGDYKEEEEIVEIDEEDAAMFEQYFKKSDDFNSLSGSYNLADKIMASIREKESQVEDMQDDEPLANEQNTSRGNISSGLKSGEGVALPEKVIKAYTTVGSILKTWTHGKLPKLFKVIPSLRNWQDVIYVTNPEEWSPHVVYEATKLFVSNLTAKESQKFINLILLERFRDNIETSEDHSLNYHIYRAVKKSLYKPSAFFKGFLFPLVETGCNVREATIAGSVLAKVSVPALHSSAALSYLLRLPFSPPTTVFIKILLDKKYALPYQTVDDCVYYFMRFRILDDGSNGEDATRVLPVIWHKAFLTFAQRYKNDITQDQRDFLLETVRQRGHKDIGPEIRRELLAGASREFVDPQEANDDLMIDVN | |
| 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 |
|---|---|---|---|---|---|
| 19 | Acetylation | QRHDPLLKDLDAAQG HHCCHHHHHHHHHHH | 65.02 | 24489116 | |
| 29 | Acetylation | DAAQGTLKKINKKKL HHHHHHHHHHCHHHH | 51.98 | 25381059 | |
| 53 | Phosphorylation | AANEEDGYIDSKASR HCCCCCCCCCHHHHH | 17.55 | 27017623 | |
| 57 | Acetylation | EDGYIDSKASRKILQ CCCCCCHHHHHHHHH | 46.78 | 24489116 | |
| 81 | Phosphorylation | EGEELAESERNKQFE CHHHHHHHHHHHHHH | 35.93 | 24961812 | |
| 85 | Ubiquitination | LAESERNKQFEARFT HHHHHHHHHHHHEEE | 63.69 | 23749301 | |
| 147 | Phosphorylation | FEQYFKKSDDFNSLS HHHHHHHCCCHHCCC | 42.90 | 28889911 | |
| 152 | Phosphorylation | KKSDDFNSLSGSYNL HHCCCHHCCCCCCCH | 24.73 | 24961812 | |
| 154 | Phosphorylation | SDDFNSLSGSYNLAD CCCHHCCCCCCCHHH | 26.05 | 24961812 | |
| 156 | Phosphorylation | DFNSLSGSYNLADKI CHHCCCCCCCHHHHH | 13.89 | 28889911 | |
| 157 | Phosphorylation | FNSLSGSYNLADKIM HHCCCCCCCHHHHHH | 20.09 | 24961812 | |
| 172 | Phosphorylation | ASIREKESQVEDMQD HHHHHHHHHCCCCCC | 51.06 | 22369663 | |
| 189 | Phosphorylation | PLANEQNTSRGNISS CCCCCCCCCCCCCCC | 21.35 | 20377248 | |
| 190 | Phosphorylation | LANEQNTSRGNISSG CCCCCCCCCCCCCCC | 45.82 | 25521595 | |
| 195 | Phosphorylation | NTSRGNISSGLKSGE CCCCCCCCCCCCCCC | 23.50 | 22369663 | |
| 196 | Phosphorylation | TSRGNISSGLKSGEG CCCCCCCCCCCCCCC | 44.33 | 22369663 | |
| 209 | Acetylation | EGVALPEKVIKAYTT CCCCCCHHHHHHHHC | 47.52 | 24489116 | |
| 222 | Acetylation | TTVGSILKTWTHGKL HCHHHHHHHCCCCCH | 40.10 | 24489116 | |
| 234 | Acetylation | GKLPKLFKVIPSLRN CCHHHHHHHCHHCCC | 50.09 | 24489116 | |
| 310 | Phosphorylation | IYRAVKKSLYKPSAF HHHHHHHHHCCCCHH | 31.08 | 28889911 | |
| 313 | Acetylation | AVKKSLYKPSAFFKG HHHHHHCCCCHHHHH | 37.48 | 24489116 | |
| 336 | Phosphorylation | GCNVREATIAGSVLA CCCHHHHHHCHHHHH | 13.45 | 23749301 | |
| 344 | Ubiquitination | IAGSVLAKVSVPALH HCHHHHHCCCHHHCC | 30.77 | 23749301 | |
| 357 | Phosphorylation | LHSSAALSYLLRLPF CCCHHHHHHHHCCCC | 14.70 | 30377154 | |
| 404 | Phosphorylation | FRILDDGSNGEDATR EEECCCCCCCCCHHH | 48.97 | 25752575 | |
| 465 | Phosphorylation | RELLAGASREFVDPQ HHHHHCCCCCCCCHH | 31.27 | 27214570 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ENP1_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 ENP1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-156; SER-172 ANDSER-404, 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-172, AND MASSSPECTROMETRY. | |
