| UniProt ID | CET1_YEAST | |
|---|---|---|
| UniProt AC | O13297 | |
| Protein Name | mRNA-capping enzyme subunit beta | |
| Gene Name | CET1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 549 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.. | |
| Protein Sequence | MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPDRVNPPVSSQCVFTELDAHLTPNIDASLFKELSKYIRGISEVTENTGKFSIIESQTRDSVYRVGLSTQRPRFLRMSTDIKTGRVGQFIEKRHVAQLLLYSPKDSYDVKISLNLELPVPDNDPPEKYKSQSPISERTKDRVSYIHNDSCTRIDITKVENHNQNSKSRQSETTHEVELEINTPALLNAFDNITNDSKEYASLIRTFLNNGTIIRRKLSSLSYEIFEGSKKVM | |
| 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 | Acetylation | ------MSYTDNPPQ ------CCCCCCCHH | 36.42 | 22814378 | |
| 2 | Phosphorylation | ------MSYTDNPPQ ------CCCCCCCHH | 36.42 | 30377154 | |
| 3 | Phosphorylation | -----MSYTDNPPQT -----CCCCCCCHHH | 19.47 | 28889911 | |
| 4 | Phosphorylation | ----MSYTDNPPQTK ----CCCCCCCHHHC | 23.22 | 28889911 | |
| 10 | Phosphorylation | YTDNPPQTKRALSLD CCCCCHHHCCCCCHH | 28.42 | 28889911 | |
| 11 | Acetylation | TDNPPQTKRALSLDD CCCCHHHCCCCCHHH | 30.35 | 25381059 | |
| 15 | Phosphorylation | PQTKRALSLDDLVNH HHHCCCCCHHHHHCC | 28.86 | 22369663 | |
| 27 | Acetylation | VNHDENEKVKLQKLS HCCCCCCCHHHHHHH | 57.14 | 24489116 | |
| 32 | Acetylation | NEKVKLQKLSEAANG CCCHHHHHHHHHHCC | 65.50 | 24489116 | |
| 34 | Phosphorylation | KVKLQKLSEAANGSR CHHHHHHHHHHCCCC | 32.02 | 22369663 | |
| 40 | Phosphorylation | LSEAANGSRPFAENL HHHHHCCCCCCHHHH | 36.27 | 22369663 | |
| 49 | Phosphorylation | PFAENLESDINQTET CCHHHHHCCCCCCCC | 47.13 | 22369663 | |
| 54 | Phosphorylation | LESDINQTETGQAAP HHCCCCCCCCCCCCC | 30.90 | 22369663 | |
| 56 | Phosphorylation | SDINQTETGQAAPID CCCCCCCCCCCCCCC | 37.67 | 22369663 | |
| 65 | Phosphorylation | QAAPIDNYKESTGHG CCCCCCCCHHCCCCC | 16.63 | 22369663 | |
| 75 | Phosphorylation | STGHGSHSQKPKSRK CCCCCCCCCCCCCCC | 41.41 | 30377154 | |
| 77 | Acetylation | GHGSHSQKPKSRKSS CCCCCCCCCCCCCCC | 58.38 | 25381059 | |
| 121 | Phosphorylation | KQHRNLLSNGSPPMN HHHHHHHHCCCCCCC | 42.16 | 22369663 | |
| 124 | Phosphorylation | RNLLSNGSPPMNDGS HHHHHCCCCCCCCCC | 30.04 | 22369663 | |
| 131 | Phosphorylation | SPPMNDGSDANAKLE CCCCCCCCCCCCCCC | 36.09 | 22369663 | |
| 136 | Acetylation | DGSDANAKLEKPSDD CCCCCCCCCCCCCCC | 57.92 | 24489116 | |
| 141 | Phosphorylation | NAKLEKPSDDSIHQN CCCCCCCCCCCCCCC | 66.18 | 29136822 | |
| 144 | Phosphorylation | LEKPSDDSIHQNSKS CCCCCCCCCCCCCCC | 27.28 | 19823750 | |
| 149 | Phosphorylation | DDSIHQNSKSDEEQR CCCCCCCCCCHHHHC | 27.28 | 25005228 | |
| 151 | Phosphorylation | SIHQNSKSDEEQRIP CCCCCCCCHHHHCCC | 50.50 | 19823750 | |
| 159 | Acetylation | DEEQRIPKQGNEGNI HHHHCCCCCCCCCCC | 69.35 | 25381059 | |
| 168 | Phosphorylation | GNEGNIASNYITQVP CCCCCCCHHHCCCCC | 26.77 | 30377154 | |
| 170 | Phosphorylation | EGNIASNYITQVPLQ CCCCCHHHCCCCCCC | 11.66 | 30377154 | |
| 193 | Phosphorylation | IAGNAVGSVVKKEEE HCCHHHHHHHHHHHH | 19.69 | 30377154 | |
| 237 | Acetylation | NEISASSKPSKYRNV HHHHCCCCCHHCCCC | 51.30 | 24489116 | |
| 240 | Acetylation | SASSKPSKYRNVPIW HCCCCCHHCCCCCCH | 57.67 | 24489116 | |
| 250 | Acetylation | NVPIWAQKWKPTIKA CCCCHHHCCHHHHHH | 49.81 | 24489116 | |
| 260 | Phosphorylation | PTIKALQSINVKDLK HHHHHHHHCCCCCCC | 19.58 | 30377154 | |
| 264 | Acetylation | ALQSINVKDLKIDPS HHHHCCCCCCCCCHH | 53.51 | 24489116 | |
| 352 | Phosphorylation | ASLFKELSKYIRGIS HHHHHHHHHHHHCHH | 25.22 | 28889911 | |
| 354 | Phosphorylation | LFKELSKYIRGISEV HHHHHHHHHHCHHHH | 7.77 | 28889911 | |
| 409 | Acetylation | RVGQFIEKRHVAQLL CCHHHHHHHHHHHEE | 42.88 | 24489116 | |
| 421 | Acetylation | QLLLYSPKDSYDVKI HEEEECCCCCCEEEE | 54.06 | 24489116 | |
| 444 | Acetylation | PDNDPPEKYKSQSPI CCCCCCHHHHCCCCC | 64.85 | 24489116 | |
| 449 | Phosphorylation | PEKYKSQSPISERTK CHHHHCCCCCCHHHC | 31.15 | 25752575 | |
| 535 | Phosphorylation | TIIRRKLSSLSYEIF CCCEEHHHHCCHHHH | 32.06 | 30377154 | |
| 536 | Phosphorylation | IIRRKLSSLSYEIFE CCEEHHHHCCHHHHC | 31.60 | 30377154 | |
| 538 | Phosphorylation | RRKLSSLSYEIFEGS EEHHHHCCHHHHCCC | 23.75 | 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 CET1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CET1_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 CET1_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-15; SER-121; SER-124 ANDSER-144, 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 SER-15, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY. | |
