| UniProt ID | CDC10_YEAST | |
|---|---|---|
| UniProt AC | P25342 | |
| Protein Name | Cell division control protein 10 | |
| Gene Name | CDC10 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 322 | |
| Subcellular Localization |
Membrane Peripheral membrane protein . Bud neck . Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate. |
|
| Protein Description | Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.. | |
| Protein Sequence | MDPLSSVQPASYVGFDTITNQIEHRLLKKGFQFNIMVVGQSGLGKSTLINTLFASHLIDSATGDDISALPVTKTTEMKISTHTLVEDRVRLNINVIDTPGFGDFIDNSKAWEPIVKYIKEQHSQYLRKELTAQRERFITDTRVHAILYFLQPNGKELSRLDVEALKRLTEIANVIPVIGKSDTLTLDERTEFRELIQNEFEKYNFKIYPYDSEELTDEELELNRSVRSIIPFAVVGSENEIEINGETFRGRKTRWSAINVEDINQCDFVYLREFLIRTHLQDLIETTSYIHYEGFRARQLIALKENANSRSSAHMSSNAIQR | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDPLSSVQ -------CCCHHHCC | 12.35 | 22814378 | |
| 5 | Phosphorylation | ---MDPLSSVQPASY ---CCCHHHCCCCHH | 33.57 | 24961812 | |
| 6 | Phosphorylation | --MDPLSSVQPASYV --CCCHHHCCCCHHC | 32.24 | 24961812 | |
| 11 | Phosphorylation | LSSVQPASYVGFDTI HHHCCCCHHCCHHHH | 27.34 | 30377154 | |
| 17 | Phosphorylation | ASYVGFDTITNQIEH CHHCCHHHHHHHHHH | 27.69 | 30377154 | |
| 19 | Phosphorylation | YVGFDTITNQIEHRL HCCHHHHHHHHHHHH | 24.14 | 30377154 | |
| 67 | Phosphorylation | SATGDDISALPVTKT CCCCCCCCCCCCCCC | 30.65 | 28889911 | |
| 73 | Acetylation | ISALPVTKTTEMKIS CCCCCCCCCCEEEEE | 54.40 | 21984913 | |
| 73 | Ubiquitination | ISALPVTKTTEMKIS CCCCCCCCCCEEEEE | 54.40 | 24961812 | |
| 78 | Acetylation | VTKTTEMKISTHTLV CCCCCEEEEEECEEE | 27.54 | 21984913 | |
| 98 | Phosphorylation | LNINVIDTPGFGDFI ECEEEECCCCCHHHC | 17.75 | 27214570 | |
| 108 | Phosphorylation | FGDFIDNSKAWEPIV CHHHCCCCCCHHHHH | 21.72 | 27214570 | |
| 116 | Acetylation | KAWEPIVKYIKEQHS CCHHHHHHHHHHHHH | 41.81 | 24489116 | |
| 119 | Ubiquitination | EPIVKYIKEQHSQYL HHHHHHHHHHHHHHH | 48.51 | 23749301 | |
| 119 | Acetylation | EPIVKYIKEQHSQYL HHHHHHHHHHHHHHH | 48.51 | 22865919 | |
| 128 | Acetylation | QHSQYLRKELTAQRE HHHHHHHHHHHHHHH | 55.25 | 21984913 | |
| 155 | Acetylation | YFLQPNGKELSRLDV EEECCCCCCHHHCCH | 63.22 | 24489116 | |
| 155 | Ubiquitination | YFLQPNGKELSRLDV EEECCCCCCHHHCCH | 63.22 | 24961812 | |
| 166 | Acetylation | RLDVEALKRLTEIAN HCCHHHHHHHHHHHH | 53.03 | 24489116 | |
| 202 | Acetylation | LIQNEFEKYNFKIYP HHHHHHHHCCCEEEC | 51.30 | 24489116 | |
| 208 | Phosphorylation | EKYNFKIYPYDSEEL HHCCCEEECCCCHHC | 9.06 | 26447709 | |
| 210 | Phosphorylation | YNFKIYPYDSEELTD CCCEEECCCCHHCCH | 18.35 | 26447709 | |
| 212 | Phosphorylation | FKIYPYDSEELTDEE CEEECCCCHHCCHHH | 27.42 | 28889911 | |
| 216 | Phosphorylation | PYDSEELTDEELELN CCCCHHCCHHHHHHH | 44.65 | 22369663 | |
| 304 | Acetylation | ARQLIALKENANSRS HHHHHHHHHCCCCCC | 39.64 | 25381059 | |
| 309 | Phosphorylation | ALKENANSRSSAHMS HHHHCCCCCCCCCHH | 31.00 | 22369663 | |
| 311 | Phosphorylation | KENANSRSSAHMSSN HHCCCCCCCCCHHCC | 31.53 | 22369663 | |
| 312 | Phosphorylation | ENANSRSSAHMSSNA HCCCCCCCCCHHCCC | 22.53 | 22369663 | |
| 314 | Phosphorylation | ANSRSSAHMSSNAIQ CCCCCCCCHHCCCCC | 20.71 | - | |
| 316 | Phosphorylation | SRSSAHMSSNAIQR- CCCCCCHHCCCCCC- | 15.58 | 22369663 | |
| 317 | Phosphorylation | RSSAHMSSNAIQR-- CCCCCHHCCCCCC-- | 23.78 | 22369663 |
| 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 CDC10_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC10_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 CDC10_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "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 HIS-314, AND MASSSPECTROMETRY. | |
| "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-67; THR-216; SER-311;SER-312 AND SER-317, 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-312 AND SER-316, ANDMASS 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-216, AND MASSSPECTROMETRY. | |
