| UniProt ID | CDC3_YEAST | |
|---|---|---|
| UniProt AC | P32457 | |
| Protein Name | Cell division control protein 3 | |
| Gene Name | CDC3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 520 | |
| 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 | MSLKEEQVSIKQDPEQEERQHDQFNDVQIKQESQDHDGVDSQYTNGTQNDDSERFEAAESDVKVEPGLGMGITSSQSEKGQVLPDQPEIKFIRRQINGYVGFANLPKQWHRRSIKNGFSFNLLCVGPDGIGKTTLMKTLFNNDDIEANLVKDYEEELANDQEEEEGQGEGHENQSQEQRHKVKIKSYESVIEENGVKLNLNVIDTEGFGDFLNNDQKSWDPIIKEIDSRFDQYLDAENKINRHSINDKRIHACLYFIEPTGHYLKPLDLKFMQSVYEKCNLIPVIAKSDILTDEEILSFKKTIMNQLIQSNIELFKPPIYSNDDAENSHLSERLFSSLPYAVIGSNDIVENYSGNQVRGRSYPWGVIEVDNDNHSDFNLLKNLLIKQFMEELKERTSKILYENYRSSKLAKLGIKQDNSVFKEFDPISKQQEEKTLHEAKLAKLEIEMKTVFQQKVSEKEKKLQKSETELFARHKEMKEKLTKQLKALEDKKKQLELSINSASPNVNHSPVPTKKKGFLR | |
| 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 | ------MSLKEEQVS ------CCCHHHHCC | 48.42 | 22369663 | |
| 2 | Acetylation | ------MSLKEEQVS ------CCCHHHHCC | 48.42 | 22814378 | |
| 4 | Sumoylation | ----MSLKEEQVSIK ----CCCHHHHCCCC | 52.47 | - | |
| 4 | Sumoylation | ----MSLKEEQVSIK ----CCCHHHHCCCC | 52.47 | 15166219 | |
| 4 | Acetylation | ----MSLKEEQVSIK ----CCCHHHHCCCC | 52.47 | 24489116 | |
| 4 | Ubiquitination | ----MSLKEEQVSIK ----CCCHHHHCCCC | 52.47 | 24961812 | |
| 9 | Phosphorylation | SLKEEQVSIKQDPEQ CCHHHHCCCCCCHHH | 24.62 | 22369663 | |
| 11 | Sumoylation | KEEQVSIKQDPEQEE HHHHCCCCCCHHHHH | 40.94 | - | |
| 11 | Sumoylation | KEEQVSIKQDPEQEE HHHHCCCCCCHHHHH | 40.94 | - | |
| 11 | Acetylation | KEEQVSIKQDPEQEE HHHHCCCCCCHHHHH | 40.94 | 24489116 | |
| 11 | Ubiquitination | KEEQVSIKQDPEQEE HHHHCCCCCCHHHHH | 40.94 | 23749301 | |
| 30 | Ubiquitination | QFNDVQIKQESQDHD CCCCCCHHHHCCCCC | 30.81 | - | |
| 30 | Sumoylation | QFNDVQIKQESQDHD CCCCCCHHHHCCCCC | 30.81 | - | |
| 30 | Sumoylation | QFNDVQIKQESQDHD CCCCCCHHHHCCCCC | 30.81 | - | |
| 33 | Phosphorylation | DVQIKQESQDHDGVD CCCHHHHCCCCCCCC | 38.11 | 20377248 | |
| 41 | Phosphorylation | QDHDGVDSQYTNGTQ CCCCCCCCCCCCCCC | 23.76 | 20377248 | |
| 43 | Phosphorylation | HDGVDSQYTNGTQND CCCCCCCCCCCCCCC | 13.21 | 20377248 | |
| 44 | Phosphorylation | DGVDSQYTNGTQNDD CCCCCCCCCCCCCCH | 21.38 | 22369663 | |
| 47 | Phosphorylation | DSQYTNGTQNDDSER CCCCCCCCCCCHHHH | 26.69 | 22369663 | |
| 52 | Phosphorylation | NGTQNDDSERFEAAE CCCCCCHHHHHHHHH | 33.27 | 20377248 | |
| 60 | Phosphorylation | ERFEAAESDVKVEPG HHHHHHHCCCCCCCC | 42.87 | 22369663 | |
| 63 | Sumoylation | EAAESDVKVEPGLGM HHHHCCCCCCCCCCC | 45.96 | - | |
| 63 | Ubiquitination | EAAESDVKVEPGLGM HHHHCCCCCCCCCCC | 45.96 | 15542864 | |
| 63 | Sumoylation | EAAESDVKVEPGLGM HHHHCCCCCCCCCCC | 45.96 | - | |
| 73 | Phosphorylation | PGLGMGITSSQSEKG CCCCCCCCCCCCCCC | 19.32 | 22369663 | |
| 74 | Phosphorylation | GLGMGITSSQSEKGQ CCCCCCCCCCCCCCC | 25.18 | 22890988 | |
| 75 | Phosphorylation | LGMGITSSQSEKGQV CCCCCCCCCCCCCCC | 29.13 | 22369663 | |
| 77 | Phosphorylation | MGITSSQSEKGQVLP CCCCCCCCCCCCCCC | 43.13 | 22369663 | |
| 90 | Acetylation | LPDQPEIKFIRRQIN CCCCHHHHHHHHHHC | 32.83 | 24489116 | |
| 90 | Ubiquitination | LPDQPEIKFIRRQIN CCCCHHHHHHHHHHC | 32.83 | 24961812 | |
| 99 | Phosphorylation | IRRQINGYVGFANLP HHHHHCCEECCCCCC | 7.91 | 27017623 | |
| 107 | Acetylation | VGFANLPKQWHRRSI ECCCCCCHHHHHHHC | 70.01 | 24489116 | |
| 119 | Phosphorylation | RSIKNGFSFNLLCVG HHCCCCCCEEEEEEC | 18.02 | 30377154 | |
| 137 | Acetylation | IGKTTLMKTLFNNDD CCHHHHHHHHCCCCC | 45.23 | 21984913 | |
| 153 | Phosphorylation | EANLVKDYEEELAND HHHHHHHHHHHHHCC | 21.37 | 22369663 | |
| 175 | Phosphorylation | GEGHENQSQEQRHKV CCCCCCCCHHHHHCC | 47.46 | 22369663 | |
| 224 | Acetylation | KSWDPIIKEIDSRFD CCCHHHHHHHHHHHH | 49.70 | 24489116 | |
| 239 | Acetylation | QYLDAENKINRHSIN HHHCHHCCCCCCCCC | 32.63 | 24489116 | |
| 274 | Phosphorylation | LDLKFMQSVYEKCNL HCHHHHHHHHHHCCC | 18.19 | 27017623 | |
| 276 | Phosphorylation | LKFMQSVYEKCNLIP HHHHHHHHHHCCCHH | 18.21 | 27017623 | |
| 287 | Sumoylation | NLIPVIAKSDILTDE CCHHHCCCCCCCCHH | 37.22 | - | |
| 287 | Sumoylation | NLIPVIAKSDILTDE CCHHHCCCCCCCCHH | 37.22 | - | |
| 300 | Acetylation | DEEILSFKKTIMNQL HHHHHHHHHHHHHHH | 45.70 | 24489116 | |
| 316 | Acetylation | QSNIELFKPPIYSND HHCCHHHCCCCCCCC | 63.61 | 21984913 | |
| 336 | Phosphorylation | HLSERLFSSLPYAVI CHHHHHHHCCCEEEE | 35.24 | 28889911 | |
| 337 | Phosphorylation | LSERLFSSLPYAVIG HHHHHHHCCCEEEEC | 26.48 | 28889911 | |
| 386 | Acetylation | LLKNLLIKQFMEELK HHHHHHHHHHHHHHH | 37.14 | 24489116 | |
| 393 | Acetylation | KQFMEELKERTSKIL HHHHHHHHHHHHHHH | 48.72 | 24489116 | |
| 396 | Phosphorylation | MEELKERTSKILYEN HHHHHHHHHHHHHHH | 35.15 | 28889911 | |
| 398 | Acetylation | ELKERTSKILYENYR HHHHHHHHHHHHHHH | 35.80 | 24489116 | |
| 415 | Ubiquitination | KLAKLGIKQDNSVFK HHHHHCCCCCCCHHH | 50.21 | 23749301 | |
| 419 | Phosphorylation | LGIKQDNSVFKEFDP HCCCCCCCHHHHCCC | 36.90 | 23749301 | |
| 422 | Acetylation | KQDNSVFKEFDPISK CCCCCHHHHCCCCCH | 56.14 | 24489116 | |
| 440 | Acetylation | EKTLHEAKLAKLEIE HHHHHHHHHHHHHHH | 46.09 | 25381059 | |
| 443 | Sumoylation | LHEAKLAKLEIEMKT HHHHHHHHHHHHHHH | 58.02 | - | |
| 443 | Acetylation | LHEAKLAKLEIEMKT HHHHHHHHHHHHHHH | 58.02 | 24489116 | |
| 455 | Acetylation | MKTVFQQKVSEKEKK HHHHHHHHCCHHHHH | 36.62 | 25381059 | |
| 465 | Sumoylation | EKEKKLQKSETELFA HHHHHHHHHHHHHHH | 61.77 | - | |
| 465 | Acetylation | EKEKKLQKSETELFA HHHHHHHHHHHHHHH | 61.77 | 24489116 | |
| 466 | Phosphorylation | KEKKLQKSETELFAR HHHHHHHHHHHHHHH | 36.47 | 22369663 | |
| 468 | Phosphorylation | KKLQKSETELFARHK HHHHHHHHHHHHHHH | 45.11 | 22369663 | |
| 498 | Phosphorylation | KKKQLELSINSASPN HHHHHHHHCCCCCCC | 15.45 | 22369663 | |
| 501 | Phosphorylation | QLELSINSASPNVNH HHHHHCCCCCCCCCC | 28.58 | 22369663 | |
| 503 | Phosphorylation | ELSINSASPNVNHSP HHHCCCCCCCCCCCC | 19.48 | 22369663 | |
| 509 | Phosphorylation | ASPNVNHSPVPTKKK CCCCCCCCCCCCCCC | 23.53 | 22369663 | |
| 513 | Phosphorylation | VNHSPVPTKKKGFLR CCCCCCCCCCCCCCC | 56.59 | 22369663 | |
| 514 | Acetylation | NHSPVPTKKKGFLR- CCCCCCCCCCCCCC- | 46.55 | 25381059 | |
| 514 | Ubiquitination | NHSPVPTKKKGFLR- CCCCCCCCCCCCCC- | 46.55 | 23749301 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC3_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 CDC3_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-9; SER-75; SER-77;SER-175; THR-468 AND SER-509, 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-9; THR-73 AND SER-175,AND MASS SPECTROMETRY. | |
| "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-9, AND MASSSPECTROMETRY. | |
| Sumoylation | |
| Reference | PubMed |
| "A proteomic strategy for gaining insights into protein sumoylation inyeast."; Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,Gygi S.P.; Mol. Cell. Proteomics 4:246-254(2005). Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND MASS SPECTROMETRY. | |
| "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.Induction of protein sumoylation by cellular stresses."; Zhou W., Ryan J.J., Zhou H.; J. Biol. Chem. 279:32262-32268(2004). Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND MASS SPECTROMETRY. | |
| "Cell cycle-regulated attachment of the ubiquitin-related protein SUMOto the yeast septins."; Johnson E.S., Blobel G.; J. Cell Biol. 147:981-994(1999). Cited for: SUMOYLATION AT LYS-4; LYS-11; LYS-30; LYS-63 AND LYS-287, MUTAGENESISOF LYS-4; LYS-11; LYS-287; LYS-415 AND LYS-443, AND MASS SPECTROMETRY. | |
