| UniProt ID | CDC14_YEAST | |
|---|---|---|
| UniProt AC | Q00684 | |
| Protein Name | Tyrosine-protein phosphatase CDC14 | |
| Gene Name | CDC14 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 551 | |
| Subcellular Localization | Nucleus, nucleolus. Cytoplasm. Bud neck. Sequestered in the nucleolus for most of the cell cycle by the nucleolar proteins NET1 and TOF2, and is released into the nucleus and cytoplasm during anaphase. CDC55 maintains CDC14 sequestration in the nucle | |
| Protein Description | Protein phosphatase which antagonizes mitotic cyclin-dependent kinase CDC28, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Inhibits transcription of ribosomal genes (rDNA) during anaphase and controls segregation of nucleolus by facilitating condensin targeting to rDNA chromatin in anaphase. Dephosphorylates SIC1, a CDC28 inhibitor, and SWI5, a transcription factor for SIC1, and induces degradation of mitotic cyclins, likely by dephosphorylating the activator of mitotic cyclin degradation, CDH1. Dephosphorylates the microtubule bundling factor ASE1 which is required to define a centered and focused mitotic spindle midzone that can drive continuous spindle elongation. Dephosphorylates the anaphase-promoting complex inhibitor ACM1, leading to its degradation. Facilitates INN1-CYK3 complex formation which promotes cytokinesis through the dephosphorylation of CDC28-phosphosphorylated INN1. Reverts also the inhibitory CDC28 phosphorylation of CHS2 for endoplasmic reticulum export, ensuring that septum formation is contingent upon chromosome separation and exit from mitosis. Additional substrates for CDC14 are the formins BNI1 and BNR1, as well as CDC6, DBP2, DSN1, INCENP, KAR9, MCM3, ORC2, ORC6, SLD2, and SWI6. Activity is inhibited by interaction with NET1 which sequesters it to the nucleolus.. | |
| Protein Sequence | MRRSVYLDNTIEFLRGRVYLGAYDYTPEDTDELVFFTVEDAIFYNSFHLDFGPMNIGHLYRFAVIFHEILNDPENANKAVVFYSSASTRQRANAACMLCCYMILVQAWTPHQVLQPLAQVDPPFMPFRDAGYSNADFEITIQDVVYGVWRAKEKGLIDLHSFNLESYEKYEHVEFGDFNVLTPDFIAFASPQEDHPKGYLATKSSHLNQPFKSVLNFFANNNVQLVVRLNSHLYNKKHFEDIGIQHLDLIFEDGTCPDLSIVKNFVGAAETIIKRGGKIAVHCKAGLGRTGCLIGAHLIYTYGFTANECIGFLRFIRPGMVVGPQQHWLYLHQNDFREWKYTTRISLKPSEAIGGLYPLISLEEYRLQKKKLKDDKRVAQNNIEGELRDLTMTPPSNGHGALSARNSSQPSTANNGSNSFKSSAVPQTSPGQPRKGQNGSNTIEDINNNRNPTSHANRKVVIESNNSDDESMQDTNGTSNHYPKVSRKKNDISSASSSRMEDNEPSATNINNAADDTILRQLLPKNRRVTSGRRTTSAAGGIRKISGSIKK | |
| 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 |
|---|---|---|---|---|---|
| 101 | Phosphorylation | AACMLCCYMILVQAW HHHHHHHHHHHHHCC | 6.03 | 19779198 | |
| 109 | Phosphorylation | MILVQAWTPHQVLQP HHHHHCCCHHHHHHH | 17.57 | 19779198 | |
| 271 | Phosphorylation | NFVGAAETIIKRGGK HHHHHHHHHHHCCCE | 24.23 | 17563356 | |
| 341 | Phosphorylation | NDFREWKYTTRISLK CCCCCCEEEEEEEEC | 17.89 | 26447709 | |
| 342 | Phosphorylation | DFREWKYTTRISLKP CCCCCEEEEEEEECH | 13.08 | 26447709 | |
| 343 | Phosphorylation | FREWKYTTRISLKPS CCCCEEEEEEEECHH | 23.94 | 26447709 | |
| 391 | Phosphorylation | EGELRDLTMTPPSNG CCCEEECCCCCCCCC | 24.24 | 23749301 | |
| 393 | Phosphorylation | ELRDLTMTPPSNGHG CEEECCCCCCCCCCC | 27.15 | 28152593 | |
| 396 | Phosphorylation | DLTMTPPSNGHGALS ECCCCCCCCCCCCCC | 57.56 | 21440633 | |
| 407 | Phosphorylation | GALSARNSSQPSTAN CCCCCCCCCCCCCCC | 25.46 | 21440633 | |
| 408 | Phosphorylation | ALSARNSSQPSTANN CCCCCCCCCCCCCCC | 50.05 | 23749301 | |
| 411 | Phosphorylation | ARNSSQPSTANNGSN CCCCCCCCCCCCCCC | 32.30 | 28889911 | |
| 412 | Phosphorylation | RNSSQPSTANNGSNS CCCCCCCCCCCCCCC | 39.84 | 23749301 | |
| 417 | Phosphorylation | PSTANNGSNSFKSSA CCCCCCCCCCCCCCC | 31.27 | 22369663 | |
| 419 | Phosphorylation | TANNGSNSFKSSAVP CCCCCCCCCCCCCCC | 35.43 | 22369663 | |
| 422 | Phosphorylation | NGSNSFKSSAVPQTS CCCCCCCCCCCCCCC | 22.86 | 22890988 | |
| 423 | Phosphorylation | GSNSFKSSAVPQTSP CCCCCCCCCCCCCCC | 33.60 | 22890988 | |
| 428 | Phosphorylation | KSSAVPQTSPGQPRK CCCCCCCCCCCCCCC | 30.71 | 22890988 | |
| 429 | Phosphorylation | SSAVPQTSPGQPRKG CCCCCCCCCCCCCCC | 23.06 | 22369663 | |
| 440 | Phosphorylation | PRKGQNGSNTIEDIN CCCCCCCCCCHHHHH | 38.05 | 30377154 | |
| 442 | Phosphorylation | KGQNGSNTIEDINNN CCCCCCCCHHHHHCC | 27.69 | 21440633 | |
| 464 | Phosphorylation | NRKVVIESNNSDDES CCCEEEECCCCCCCH | 30.13 | 22369663 | |
| 467 | Phosphorylation | VVIESNNSDDESMQD EEEECCCCCCCHHCC | 51.17 | 22369663 | |
| 471 | Phosphorylation | SNNSDDESMQDTNGT CCCCCCCHHCCCCCC | 28.83 | 20377248 | |
| 475 | Phosphorylation | DDESMQDTNGTSNHY CCCHHCCCCCCCCCC | 20.75 | 22369663 | |
| 478 | Phosphorylation | SMQDTNGTSNHYPKV HHCCCCCCCCCCCCC | 28.55 | 29136822 | |
| 479 | Phosphorylation | MQDTNGTSNHYPKVS HCCCCCCCCCCCCCC | 24.02 | 21440633 | |
| 482 | Phosphorylation | TNGTSNHYPKVSRKK CCCCCCCCCCCCCCC | 14.70 | 21440633 | |
| 493 | Phosphorylation | SRKKNDISSASSSRM CCCCCCCCCCCCCCC | 23.79 | 21440633 | |
| 494 | Phosphorylation | RKKNDISSASSSRME CCCCCCCCCCCCCCC | 32.29 | 21440633 | |
| 496 | Phosphorylation | KNDISSASSSRMEDN CCCCCCCCCCCCCCC | 30.69 | 28889911 | |
| 497 | Phosphorylation | NDISSASSSRMEDNE CCCCCCCCCCCCCCC | 22.98 | 21440633 | |
| 498 | Phosphorylation | DISSASSSRMEDNEP CCCCCCCCCCCCCCC | 32.90 | 21440633 | |
| 531 | Phosphorylation | PKNRRVTSGRRTTSA CCCCCCCCCCCCCCC | 27.69 | 19221193 | |
| 535 | Phosphorylation | RVTSGRRTTSAAGGI CCCCCCCCCCCCCCH | 24.60 | 27214570 | |
| 536 | Phosphorylation | VTSGRRTTSAAGGIR CCCCCCCCCCCCCHH | 17.98 | 30377154 | |
| 537 | Phosphorylation | TSGRRTTSAAGGIRK CCCCCCCCCCCCHHH | 18.60 | 19221193 | |
| 546 | Phosphorylation | AGGIRKISGSIKK-- CCCHHHCCCCCCC-- | 29.53 | 19221193 | |
| 548 | Phosphorylation | GIRKISGSIKK---- CHHHCCCCCCC---- | 25.17 | 19221193 |
| 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 CDC14_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC14_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 CDC14_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-467, 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-467, 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 THR-271, AND MASSSPECTROMETRY. | |
