| UniProt ID | FIP1_YEAST | |
|---|---|---|
| UniProt AC | P45976 | |
| Protein Name | Pre-mRNA polyadenylation factor FIP1 | |
| Gene Name | FIP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 327 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Polymerase-regulating 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. Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase PAP1. This inhibits the extension of an oligo(A) primer by limiting access of the RNA substrate to the C-terminal RNA binding domain of PAP1. Seems to tether PAP1 to the cleavage factor I.. | |
| Protein Sequence | MSSSEDEDDKFLYGSDSELALPSSKRSRDDEADAGASSNPDIVKRQKFDSPVEETPATARDDRSDEDIYSDSSDDDSDSDLEVIISLGPDPTRLDAKLLDSYSTAATSSSKDVISVATDVSNTITKTSDERLITEGEANQGVTATTVKATESDGNVPKAMTGSIDLDKEGIFDSVGITTIDPEVLKEKPWRQPGANLSDYFNYGFNEFTWMEYLHRQEKLQQDYNPRRILMGLLSLQQQGKLNSANDTDSNLGNIIDNNNNVNNANMSNLNSNMGNSMSGTPNPPAPPMHPSFPPLPMFGSFPPFPMPGMMPPMNQQPNQNQNQNSK | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSSSEDEDD ------CCCCCCCCC | 42.44 | 19795423 | |
| 3 | Phosphorylation | -----MSSSEDEDDK -----CCCCCCCCCC | 36.13 | 19795423 | |
| 4 | Phosphorylation | ----MSSSEDEDDKF ----CCCCCCCCCCC | 41.58 | 19795423 | |
| 13 | Phosphorylation | DEDDKFLYGSDSELA CCCCCCCCCCCCCCC | 20.09 | 22890988 | |
| 15 | Phosphorylation | DDKFLYGSDSELALP CCCCCCCCCCCCCCC | 25.14 | 22369663 | |
| 17 | Phosphorylation | KFLYGSDSELALPSS CCCCCCCCCCCCCCC | 35.89 | 22890988 | |
| 23 | Phosphorylation | DSELALPSSKRSRDD CCCCCCCCCCCCCCC | 49.71 | 22890988 | |
| 24 | Phosphorylation | SELALPSSKRSRDDE CCCCCCCCCCCCCCC | 30.10 | 22890988 | |
| 27 | Phosphorylation | ALPSSKRSRDDEADA CCCCCCCCCCCCCCC | 43.74 | 22369663 | |
| 37 | Phosphorylation | DEADAGASSNPDIVK CCCCCCCCCCHHHHH | 29.72 | 22369663 | |
| 38 | Phosphorylation | EADAGASSNPDIVKR CCCCCCCCCHHHHHH | 52.42 | 24909858 | |
| 44 | Acetylation | SSNPDIVKRQKFDSP CCCHHHHHHHCCCCC | 49.82 | 25381059 | |
| 47 | Acetylation | PDIVKRQKFDSPVEE HHHHHHHCCCCCCCC | 55.99 | 24489116 | |
| 50 | Phosphorylation | VKRQKFDSPVEETPA HHHHCCCCCCCCCCC | 33.70 | 22369663 | |
| 55 | Phosphorylation | FDSPVEETPATARDD CCCCCCCCCCCCCCC | 12.52 | 22890988 | |
| 58 | Phosphorylation | PVEETPATARDDRSD CCCCCCCCCCCCCCC | 24.35 | 22890988 | |
| 73 | Phosphorylation | EDIYSDSSDDDSDSD CCCCCCCCCCCCCCC | 50.48 | 28889911 | |
| 77 | Phosphorylation | SDSSDDDSDSDLEVI CCCCCCCCCCCCEEE | 46.11 | 28889911 | |
| 101 | Phosphorylation | LDAKLLDSYSTAATS HCHHHHHHHCCCCCC | 22.43 | 19823750 | |
| 102 | Phosphorylation | DAKLLDSYSTAATSS CHHHHHHHCCCCCCC | 15.09 | 29734811 | |
| 103 | Phosphorylation | AKLLDSYSTAATSSS HHHHHHHCCCCCCCC | 18.60 | 29734811 | |
| 104 | Phosphorylation | KLLDSYSTAATSSSK HHHHHHCCCCCCCCC | 16.45 | 29734811 | |
| 107 | Phosphorylation | DSYSTAATSSSKDVI HHHCCCCCCCCCHHE | 27.03 | 19823750 | |
| 108 | Phosphorylation | SYSTAATSSSKDVIS HHCCCCCCCCCHHEE | 28.08 | 19823750 | |
| 109 | Phosphorylation | YSTAATSSSKDVISV HCCCCCCCCCHHEEE | 36.73 | 19795423 | |
| 110 | Phosphorylation | STAATSSSKDVISVA CCCCCCCCCHHEEEE | 32.42 | 19795423 | |
| 145 | Phosphorylation | ANQGVTATTVKATES CCCCCCEEEEEEECC | 23.82 | 17563356 | |
| 152 | Phosphorylation | TTVKATESDGNVPKA EEEEEECCCCCCCCC | 46.60 | 23749301 | |
| 161 | Phosphorylation | GNVPKAMTGSIDLDK CCCCCCCEECCCCCC | 32.41 | 24961812 | |
| 163 | Phosphorylation | VPKAMTGSIDLDKEG CCCCCEECCCCCCCC | 12.08 | 24909858 | |
| 219 | Ubiquitination | EYLHRQEKLQQDYNP HHHHHHHHHHCCCCH | 43.17 | 23749301 |
| 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 FIP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FIP1_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 FIP1_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-50, AND MASSSPECTROMETRY. | |
| "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-50 AND THR-145, AND MASSSPECTROMETRY. | |
