| UniProt ID | PESC_YEAST | |
|---|---|---|
| UniProt AC | P53261 | |
| Protein Name | Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000303|PubMed:12022229} | |
| Gene Name | NOP7 {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000303|PubMed:11911362} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 605 | |
| Subcellular Localization | Nucleus, nucleolus . Nucleus, nucleoplasm. Accumulates in the nucleolus in response to rapamycin treatment. | |
| Protein Description | Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.. | |
| Protein Sequence | MRIKKKNTRGNARNFITRSQAVRKLQVSLADFRRLCIFKGIYPREPRNKKKANKGSTAPTTFYYAKDIQYLMHEPVLAKFREHKTFARKLTRALGRGEVSSAKRLEENRDSYTLDHIIKERYPSFPDAIRDIDDALNMLFLFSNLPSTNQVSSKIINDAQKICNQWLAYVAKERLVRKVFVSIKGVYYQANIKGEEVRWLVPFKFPENIPSDVDFRIMLTFLEFYSTLLHFVLYKLYTDSGLIYPPKLDLKKDKIISGLSSYILESRQEDSLLKLDPTEIEEDVKVESLDASTLKSALNADEANTDETEKEEEQEKKQEKEQEKEQNEETELDTFEDNNKNKGDILIQPSKYDSPVASLFSAFVFYVSREVPIDILEFLILSCGGNVISEAAMDQIENKKDIDMSKVTHQIVDRPVLKNKVAGRTYIQPQWIFDCINKGELVPANKYLPGEALPPHLSPWGDAIGYDPTAPVEEGEEEESESESESEDQVEEEDQEVVAGEEDDDDDEELQAQKELELEAQGIKYSETSEADKDVNKSKNKKRKVDEEEEEKKLKMIMMSNKQKKLYKKMKYSNAKKEEQAENLKKKKKQIAKQKAKLNKLDSKK | |
| 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 |
|---|---|---|---|---|---|
| 24 | Acetylation | TRSQAVRKLQVSLAD CHHHHHHHHHCCHHH | 36.35 | 24489116 | |
| 39 | Acetylation | FRRLCIFKGIYPREP HHHHHHHCCCCCCCC | 25.20 | 24489116 | |
| 60 | Phosphorylation | NKGSTAPTTFYYAKD CCCCCCCCCHHHHHH | 27.37 | 27017623 | |
| 79 | Acetylation | MHEPVLAKFREHKTF HCHHHHHHHHHHHHH | 40.57 | 24489116 | |
| 103 | Acetylation | RGEVSSAKRLEENRD CCCCCCCHHHHHCCC | 60.51 | 25381059 | |
| 119 | Acetylation | YTLDHIIKERYPSFP CCHHHHHHHHCCCCH | 35.22 | 24489116 | |
| 143 | Phosphorylation | LNMLFLFSNLPSTNQ HHHHHHHCCCCCCCC | 39.34 | 29688323 | |
| 147 | Phosphorylation | FLFSNLPSTNQVSSK HHHCCCCCCCCCHHH | 43.06 | 29688323 | |
| 148 | Phosphorylation | LFSNLPSTNQVSSKI HHCCCCCCCCCHHHH | 27.94 | 29688323 | |
| 152 | Phosphorylation | LPSTNQVSSKIINDA CCCCCCCHHHHHHHH | 19.02 | 29688323 | |
| 153 | Phosphorylation | PSTNQVSSKIINDAQ CCCCCCHHHHHHHHH | 29.08 | 29688323 | |
| 172 | Acetylation | QWLAYVAKERLVRKV HHHHHHHHHHHHHHH | 33.07 | 24489116 | |
| 254 | Acetylation | KLDLKKDKIISGLSS CCCCCCCHHHHHHHH | 51.31 | 24489116 | |
| 260 | Phosphorylation | DKIISGLSSYILESR CHHHHHHHHHHHHHC | 25.31 | 30377154 | |
| 261 | Phosphorylation | KIISGLSSYILESRQ HHHHHHHHHHHHHCC | 22.64 | 28889911 | |
| 262 | Phosphorylation | IISGLSSYILESRQE HHHHHHHHHHHHCCC | 13.22 | 30377154 | |
| 266 | Phosphorylation | LSSYILESRQEDSLL HHHHHHHHCCCCCCC | 35.50 | 28889911 | |
| 271 | Phosphorylation | LESRQEDSLLKLDPT HHHCCCCCCCCCCHH | 34.54 | 27017623 | |
| 288 | Phosphorylation | EEDVKVESLDASTLK CCCCEEEECCHHHHH | 34.24 | 29136822 | |
| 292 | Phosphorylation | KVESLDASTLKSALN EEEECCHHHHHHHHC | 33.66 | 21551504 | |
| 293 | Phosphorylation | VESLDASTLKSALNA EEECCHHHHHHHHCC | 39.67 | 19779198 | |
| 296 | Phosphorylation | LDASTLKSALNADEA CCHHHHHHHHCCCCC | 40.89 | 28889911 | |
| 305 | Phosphorylation | LNADEANTDETEKEE HCCCCCCCCHHHHHH | 42.11 | 28152593 | |
| 308 | Phosphorylation | DEANTDETEKEEEQE CCCCCCHHHHHHHHH | 55.99 | 25521595 | |
| 310 | Acetylation | ANTDETEKEEEQEKK CCCCHHHHHHHHHHH | 77.25 | 24489116 | |
| 324 | Acetylation | KQEKEQEKEQNEETE HHHHHHHHHHHHHHC | 65.38 | 24489116 | |
| 330 | Phosphorylation | EKEQNEETELDTFED HHHHHHHHCHHHCCC | 35.35 | 28889911 | |
| 334 | Phosphorylation | NEETELDTFEDNNKN HHHHCHHHCCCCCCC | 41.36 | 28889911 | |
| 406 | Acetylation | KKDIDMSKVTHQIVD CCCCCHHHHHHHHCC | 44.51 | 24489116 | |
| 418 | Acetylation | IVDRPVLKNKVAGRT HCCCHHHCCCCCCCC | 55.76 | 22865919 | |
| 525 | Phosphorylation | LEAQGIKYSETSEAD HHHCCCCCCCCCHHH | 15.15 | 25005228 | |
| 526 | Phosphorylation | EAQGIKYSETSEADK HHCCCCCCCCCHHHH | 29.42 | 24961812 | |
| 528 | Phosphorylation | QGIKYSETSEADKDV CCCCCCCCCHHHHCC | 26.40 | 24961812 | |
| 529 | Phosphorylation | GIKYSETSEADKDVN CCCCCCCCHHHHCCC | 27.08 | 25521595 | |
| 533 | Acetylation | SETSEADKDVNKSKN CCCCHHHHCCCHHHC | 71.30 | 22865919 | |
| 537 | Acetylation | EADKDVNKSKNKKRK HHHHCCCHHHCCCCC | 63.76 | 25381059 | |
| 560 | Phosphorylation | KLKMIMMSNKQKKLY HHHHHHHCHHHHHHH | 24.40 | 27017623 | |
| 562 | Ubiquitination | KMIMMSNKQKKLYKK HHHHHCHHHHHHHHH | 57.07 | 23793018 | |
| 564 | Ubiquitination | IMMSNKQKKLYKKMK HHHCHHHHHHHHHHH | 46.48 | 23793018 | |
| 571 | Acetylation | KKLYKKMKYSNAKKE HHHHHHHHHCHHHHH | 55.17 | 25381059 | |
| 585 | Acetylation | EEQAENLKKKKKQIA HHHHHHHHHHHHHHH | 74.30 | 25381059 | |
| 600 | Acetylation | KQKAKLNKLDSKK-- HHHHHHHHHHCCC-- | 65.20 | 25381059 | |
| 603 | Phosphorylation | AKLNKLDSKK----- HHHHHHHCCC----- | 53.43 | 21551504 |
| 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 PESC_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PESC_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 PESC_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-261; SER-266; SER-288;THR-305; THR-308; THR-334 AND SER-529, 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 THR-308 AND SER-529, ANDMASS SPECTROMETRY. | |
