| UniProt ID | SIC1_YEAST | |
|---|---|---|
| UniProt AC | P38634 | |
| Protein Name | Protein SIC1 | |
| Gene Name | SIC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 284 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Substrate and inhibitor of the cyclin-dependent protein kinase CDC28. Its activity could be important for faithful segregation of chromosomes to daughter cells. It acts in response to a signal from a post-start checkpoint.. | |
| Protein Sequence | MTPSTPPRSRGTRYLAQPSGNTSSSALMQGQKTPQKPSQNLVPVTPSTTKSFKNAPLLAPPNSNMGMTSPFNGLTSPQRSPFPKSSVKRTLFQFESHDNGTVREEQEPLGRVNRILFPTQQNVDIDAAEEEEEGEVLLPPSRPTSARQLHLSLERDEFDQTHRKKIIKDVPGTPSDKVITFELAKNWNNNSPKNDARSQESEDEEDIIINPVRVGKNPFASDELVTQEIRNERKRAMLRENPDIEDVITYVNKKGEVVEKRRLTDEEKRRFKPKALFQSRDQEH | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTPSTPPRS ------CCCCCCCCC | 26.41 | 24909858 | |
| 4 | Phosphorylation | ----MTPSTPPRSRG ----CCCCCCCCCCC | 44.36 | 23749301 | |
| 5 | Phosphorylation | ---MTPSTPPRSRGT ---CCCCCCCCCCCC | 38.22 | 9334303 | |
| 14 | Phosphorylation | PRSRGTRYLAQPSGN CCCCCCCEEECCCCC | 13.26 | 28889911 | |
| 19 | Phosphorylation | TRYLAQPSGNTSSSA CCEEECCCCCCCHHH | 32.37 | 24909858 | |
| 22 | Phosphorylation | LAQPSGNTSSSALMQ EECCCCCCCHHHHHC | 33.25 | 22369663 | |
| 23 | Phosphorylation | AQPSGNTSSSALMQG ECCCCCCCHHHHHCC | 26.71 | 24909858 | |
| 24 | Phosphorylation | QPSGNTSSSALMQGQ CCCCCCCHHHHHCCC | 20.00 | 24909858 | |
| 25 | Phosphorylation | PSGNTSSSALMQGQK CCCCCCHHHHHCCCC | 25.78 | 22369663 | |
| 32 | Ubiquitination | SALMQGQKTPQKPSQ HHHHCCCCCCCCCCC | 69.83 | 17644757 | |
| 33 | Phosphorylation | ALMQGQKTPQKPSQN HHHCCCCCCCCCCCC | 24.06 | 9334303 | |
| 36 | Ubiquitination | QGQKTPQKPSQNLVP CCCCCCCCCCCCCEE | 48.08 | 17644757 | |
| 38 | Phosphorylation | QKTPQKPSQNLVPVT CCCCCCCCCCCEECC | 38.44 | 22369663 | |
| 45 | Phosphorylation | SQNLVPVTPSTTKSF CCCCEECCCCCCCCC | 12.88 | 22369663 | |
| 47 | Phosphorylation | NLVPVTPSTTKSFKN CCEECCCCCCCCCCC | 39.07 | 22369663 | |
| 48 | Phosphorylation | LVPVTPSTTKSFKNA CEECCCCCCCCCCCC | 39.17 | 22369663 | |
| 49 | Phosphorylation | VPVTPSTTKSFKNAP EECCCCCCCCCCCCC | 29.09 | 22369663 | |
| 50 | Ubiquitination | PVTPSTTKSFKNAPL ECCCCCCCCCCCCCC | 54.72 | 17644757 | |
| 53 | Ubiquitination | PSTTKSFKNAPLLAP CCCCCCCCCCCCCCC | 60.33 | - | |
| 69 | Phosphorylation | NSNMGMTSPFNGLTS CCCCCCCCCCCCCCC | 20.71 | 9334303 | |
| 76 | Phosphorylation | SPFNGLTSPQRSPFP CCCCCCCCCCCCCCC | 24.87 | 9334303 | |
| 80 | Phosphorylation | GLTSPQRSPFPKSSV CCCCCCCCCCCHHHH | 26.16 | 9334303 | |
| 84 | Ubiquitination | PQRSPFPKSSVKRTL CCCCCCCHHHHCEEE | 56.60 | - | |
| 88 | Ubiquitination | PFPKSSVKRTLFQFE CCCHHHHCEEEEEEE | 41.43 | - | |
| 119 | Phosphorylation | VNRILFPTQQNVDID CCEEEEECCCCCCCC | 35.14 | 22369663 | |
| 141 | Phosphorylation | GEVLLPPSRPTSARQ CCEECCCCCCCCHHH | 49.29 | 22369663 | |
| 144 | Phosphorylation | LLPPSRPTSARQLHL ECCCCCCCCHHHHHH | 33.63 | 22369663 | |
| 145 | Phosphorylation | LPPSRPTSARQLHLS CCCCCCCCHHHHHHH | 24.92 | 22369663 | |
| 173 | Phosphorylation | IIKDVPGTPSDKVIT HHHCCCCCCCCCEEE | 17.35 | 9334303 | |
| 175 | Phosphorylation | KDVPGTPSDKVITFE HCCCCCCCCCEEEEE | 50.31 | 28132839 | |
| 191 | Phosphorylation | AKNWNNNSPKNDARS HHHCCCCCCCCCCCC | 39.10 | 9334303 | |
| 198 | Phosphorylation | SPKNDARSQESEDEE CCCCCCCCCCCCCHH | 39.77 | 22369663 | |
| 201 | Phosphorylation | NDARSQESEDEEDII CCCCCCCCCCHHCCE | 42.59 | 22369663 | |
| 216 | Ubiquitination | INPVRVGKNPFASDE ECCEECCCCCCCCCH | 59.60 | 17644757 | |
| 234 | Ubiquitination | QEIRNERKRAMLREN HHHHHHHHHHHHHHC | 38.03 | 15699485 | |
| 253 | Acetylation | DVITYVNKKGEVVEK HHHHHHCCCCCEEEE | 52.70 | 24489116 | |
| 253 | Ubiquitination | DVITYVNKKGEVVEK HHHHHHCCCCCEEEE | 52.70 | 17644757 | |
| 254 | Ubiquitination | VITYVNKKGEVVEKR HHHHHCCCCCEEEEC | 55.91 | 17644757 | |
| 268 | Other | RRLTDEEKRRFKPKA CCCCHHHHHCCCCHH | 46.99 | - | |
| 268 | Lysine derivative | RRLTDEEKRRFKPKA CCCCHHHHHCCCCHH | 46.99 | - | |
| 272 | Other | DEEKRRFKPKALFQS HHHHHCCCCHHHHCC | 43.74 | - | |
| 272 | Lysine derivative | DEEKRRFKPKALFQS HHHHHCCCCHHHHCC | 43.74 | - | |
| 274 | Other | EKRRFKPKALFQSRD HHHCCCCHHHHCCCC | 59.31 | - | |
| 274 | Lysine derivative | EKRRFKPKALFQSRD HHHCCCCHHHHCCCC | 59.31 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 5 | T | Phosphorylation | Kinase | CDK1 | P00546 | GPS |
| 5 | T | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
| 33 | T | Phosphorylation | Kinase | CDK1 | P00546 | GPS |
| 45 | T | Phosphorylation | Kinase | CDK1 | P00546 | GPS |
| 48 | T | Phosphorylation | Kinase | CDK1 | P00546 | GPS |
| 69 | S | Phosphorylation | Kinase | CDK1 | P00546 | GPS |
| 76 | S | Phosphorylation | Kinase | CDK1 | P00546 | GPS |
| 80 | S | Phosphorylation | Kinase | CDK1 | P00546 | GPS |
| 201 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| - | K | Ubiquitination | E3 ubiquitin ligase | CDC4 | P07834 | PMID:9285816 |
| - | K | Ubiquitination | E3 ubiquitin ligase | GRR1 | P24814 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SIC1_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 SIC1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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 THR-5; THR-173; SER-191 ANDSER-201, AND MASS SPECTROMETRY. | |
| "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 THR-173 AND SER-201, ANDMASS 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-173 AND SER-198, ANDMASS SPECTROMETRY. | |
| "Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor,by Cdk including Pho85 kinase is required for its promptdegradation."; Nishizawa M., Kawasumi M., Fujino M., Toh-e A.; Mol. Biol. Cell 9:2393-2405(1998). Cited for: PHOSPHORYLATION AT THR-5; THR-33 AND SER-76. | |
| "Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting ofSic1."; Escote X., Zapater M., Clotet J., Posas F.; Nat. Cell Biol. 6:997-1002(2004). Cited for: FUNCTION, PHOSPHORYLATION AT THR-173, MUTAGENESIS OF THR-173, ANDINTERACTION WITH HOG1. | |
