| UniProt ID | PUS4_YEAST | |
|---|---|---|
| UniProt AC | P48567 | |
| Protein Name | tRNA pseudouridine synthase 4 | |
| Gene Name | PUS4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 403 | |
| Subcellular Localization | Nucleus . Mitochondrion . | |
| Protein Description | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. [PubMed: 9358157 Also catalyzes pseudouridylation of mRNAs with the consensus sequence 5'-GGUUCRA-3'] | |
| Protein Sequence | MNGIFAIEKPSGITSNQFMLKLQHALTKSQVFSKEIQRATAERKQQYEKQTGKKASKRKLRKVSKVKMGHGGTLDPLASGVLVIGIGAGTKKLANYLSGTVKVYESEALFGVSTTSGDVEGEILSQNSVKHLNFDDLKTVEEKFVGQLKQTPPIYAALKMDGKPLHEYAREGKPLPRAIEPRQVTIYDLKVFSDSLKRDHDYPLLRPTTEEAVDTVKNLNANMLNDVLYFSKEYTEKHGLDSEVAKVEEPFPLSEQEEQEIQKEGDSYRAPKLHFKANVSSGTYIRSLVSDIGKSMRSSCYMVKLIRLQQQDWSLEKNNVFQLTDFTERDEKVWSKVLEKVLDEGATVDVIEELKKAEKEIPADVKECIVSSDQPGDEATAETIETANAEEHSNTLKRKIEQV | |
| 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 |
|---|---|---|---|---|---|
| 28 | Acetylation | KLQHALTKSQVFSKE HHHHHHHHHHHHHHH | 39.48 | 24489116 | |
| 96 | Phosphorylation | GTKKLANYLSGTVKV CHHHHHHHHHCCEEE | 9.17 | 27017623 | |
| 100 | Phosphorylation | LANYLSGTVKVYESE HHHHHHCCEEEEECE | 17.49 | 27017623 | |
| 163 | Acetylation | AALKMDGKPLHEYAR EEEEECCEEHHHHHH | 39.89 | 25381059 | |
| 202 | Phosphorylation | SLKRDHDYPLLRPTT HCCCCCCCCCCCCCC | 7.74 | 28889911 | |
| 208 | Phosphorylation | DYPLLRPTTEEAVDT CCCCCCCCCHHHHHH | 40.17 | 27214570 | |
| 254 | Phosphorylation | VEEPFPLSEQEEQEI CCCCCCCCHHHHHHH | 37.16 | 22369663 | |
| 281 | Phosphorylation | HFKANVSSGTYIRSL EEEEECCCCHHHHHH | 30.76 | 27214570 | |
| 294 | Ubiquitination | SLVSDIGKSMRSSCY HHHHHHHHHHHHHHH | 41.22 | 24961812 | |
| 324 | Phosphorylation | KNNVFQLTDFTERDE CCCEEECCCCCHHHH | 20.48 | 27017623 | |
| 347 | Phosphorylation | KVLDEGATVDVIEEL HHHCCCCCHHHHHHH | 28.26 | 27017623 | |
| 371 | Phosphorylation | DVKECIVSSDQPGDE CHHHHEECCCCCCCH | 14.32 | 28132839 | |
| 372 | Phosphorylation | VKECIVSSDQPGDEA HHHHEECCCCCCCHH | 29.39 | 28152593 | |
| 380 | Phosphorylation | DQPGDEATAETIETA CCCCCHHHHHHHHHC | 23.99 | 19779198 | |
| 397 | Acetylation | EEHSNTLKRKIEQV- HHHHHHHHHHHHCC- | 50.00 | 25381059 |
| 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 PUS4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PUS4_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 PUS4_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-254, AND MASSSPECTROMETRY. | |