UniProt ID | PAP_YEAST | |
---|---|---|
UniProt AC | P29468 | |
Protein Name | Poly(A) polymerase | |
Gene Name | PAP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 568 | |
Subcellular Localization | Nucleus . | |
Protein Description | Polymerase 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.. | |
Protein Sequence | MSSQKVFGITGPVSTVGATAAENKLNDSLIQELKKEGSFETEQETANRVQVLKILQELAQRFVYEVSKKKNMSDGMARDAGGKIFTYGSYRLGVHGPGSDIDTLVVVPKHVTREDFFTVFDSLLRERKELDEIAPVPDAFVPIIKIKFSGISIDLICARLDQPQVPLSLTLSDKNLLRNLDEKDLRALNGTRVTDEILELVPKPNVFRIALRAIKLWAQRRAVYANIFGFPGGVAWAMLVARICQLYPNACSAVILNRFFIILSEWNWPQPVILKPIEDGPLQVRVWNPKIYAQDRSHRMPVITPAYPSMCATHNITESTKKVILQEFVRGVQITNDIFSNKKSWANLFEKNDFFFRYKFYLEITAYTRGSDEQHLKWSGLVESKVRLLVMKLEVLAGIKIAHPFTKPFESSYCCPTEDDYEMIQDKYGSHKTETALNALKLVTDENKEEESIKDAPKAYLSTMYIGLDFNIENKKEKVDIHIPCTEFVNLCRSFNEDYGDHKVFNLALRFVKGYDLPDEVFDENEKRPSKKSKRKNLDARHETVKRSKSDAASGDNINGTTAAVDVN | |
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 |
---|---|---|---|---|---|
15 | Phosphorylation | GITGPVSTVGATAAE EECCCCCHHCHHHHH | 24.16 | 28889911 | |
19 | Phosphorylation | PVSTVGATAAENKLN CCCHHCHHHHHHHCC | 22.07 | 28889911 | |
28 | Phosphorylation | AENKLNDSLIQELKK HHHHCCHHHHHHHHH | 26.71 | 30377154 | |
38 | Phosphorylation | QELKKEGSFETEQET HHHHHCCCCCCHHHH | 22.47 | 30377154 | |
444 | Phosphorylation | LNALKLVTDENKEEE HHHHHHHCCCCCCHH | 48.29 | 30377154 | |
448 | Acetylation | KLVTDENKEEESIKD HHHCCCCCCHHCHHH | 65.54 | 24489116 | |
452 | Phosphorylation | DENKEEESIKDAPKA CCCCCHHCHHHHCHH | 37.91 | 20377248 | |
503 | Acetylation | NEDYGDHKVFNLALR CCCCCCCHHHHHHHH | 53.94 | 24489116 | |
548 | Phosphorylation | RHETVKRSKSDAASG HHHHHHHHHHHHCCC | 30.69 | 28889911 | |
550 | Phosphorylation | ETVKRSKSDAASGDN HHHHHHHHHHCCCCC | 33.46 | 17850751 | |
554 | Phosphorylation | RSKSDAASGDNINGT HHHHHHCCCCCCCCC | 48.69 | 24961812 | |
561 | Phosphorylation | SGDNINGTTAAVDVN CCCCCCCCEEEEECC | 14.58 | 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 PAP_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PAP_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 PAP_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-452 AND SER-548, ANDMASS SPECTROMETRY. |