UniProt ID | PTI1_YEAST | |
---|---|---|
UniProt AC | P39927 | |
Protein Name | Protein PTI1 | |
Gene Name | PTI1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 425 | |
Subcellular Localization | Nucleus . | |
Protein Description | Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. PTI1 is required for 3'-end formation of snoRNAs.. | |
Protein Sequence | MTDPRRRTGRHFLTPENLSSTLQITNLPPEWNQDIITSVVAGSGPVIDIKAKNDPRTGKLTGVLFDYLTSKDCKRAWEILNRIENFPVKIEQIIPPNYKDHLRETANKNSQKQVLQLNRDSYPFEAGLELPFEMVTEVPIPRRPPPPQAANNTNSVSNNTNIQFPDILSKASKHLPSFQDGSIIAPDKISQNLSKIPPLQLIEIISNLKILSNQENIQKSQLESFLDTNSDITISVTQALLEMGFIDYSVVTKVLKSQVGEAPSLLSSNNTSNSNTPVSVIRNNTPLHVPSNEVSNNPNNMPLNVAMPMPMSTPPFIPLPLQQQPFGFAPPGPFMPPAQGPSMGQPVLANQLGQVQQQNISSTEGPSNANKANDSGTINMAKLQLLPENQQDMIKQVLTLTPAQIQSLPSDQQLMVENFRKEYII | |
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 |
---|---|---|---|---|---|
99 | Acetylation | QIIPPNYKDHLRETA HCCCCCHHHHHHHHC | 45.36 | 24489116 | |
105 | Phosphorylation | YKDHLRETANKNSQK HHHHHHHHCCCCCHH | 29.15 | 27017623 | |
177 | Phosphorylation | KASKHLPSFQDGSII HHHHCCCCCCCCCEE | 41.73 | 28889911 | |
182 | Phosphorylation | LPSFQDGSIIAPDKI CCCCCCCCEECCHHH | 21.07 | 30377154 | |
190 | Phosphorylation | IIAPDKISQNLSKIP EECCHHHCCCHHHCC | 20.82 | 19795423 | |
194 | Phosphorylation | DKISQNLSKIPPLQL HHHCCCHHHCCHHHH | 35.77 | 29688323 | |
257 | Phosphorylation | VVTKVLKSQVGEAPS HHHHHHHHCCCCCCH | 26.41 | 22369663 | |
264 | Phosphorylation | SQVGEAPSLLSSNNT HCCCCCCHHHCCCCC | 49.33 | 22369663 | |
267 | Phosphorylation | GEAPSLLSSNNTSNS CCCCHHHCCCCCCCC | 35.99 | 22369663 | |
268 | Phosphorylation | EAPSLLSSNNTSNSN CCCHHHCCCCCCCCC | 33.78 | 22369663 | |
271 | Phosphorylation | SLLSSNNTSNSNTPV HHHCCCCCCCCCCCE | 33.27 | 22369663 | |
272 | Phosphorylation | LLSSNNTSNSNTPVS HHCCCCCCCCCCCEE | 40.14 | 22369663 | |
274 | Phosphorylation | SSNNTSNSNTPVSVI CCCCCCCCCCCEEEE | 41.68 | 22369663 | |
276 | Phosphorylation | NNTSNSNTPVSVIRN CCCCCCCCCEEEEEC | 25.53 | 22369663 | |
279 | Phosphorylation | SNSNTPVSVIRNNTP CCCCCCEEEEECCCC | 17.03 | 22369663 | |
410 | Phosphorylation | AQIQSLPSDQQLMVE HHHHCCCCCCCHHHH | 54.03 | 30377154 |
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 PTI1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTI1_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 PTI1_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-177; SER-268; THR-271;SER-272 AND SER-274, AND MASS SPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276, AND MASSSPECTROMETRY. |