UniProt ID | CDC15_YEAST | |
---|---|---|
UniProt AC | P27636 | |
Protein Name | Cell division control protein 15 | |
Gene Name | CDC15 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 974 | |
Subcellular Localization | Cytoplasm, cytoskeleton, spindle pole. Bud neck. Localizes to the spindle pole bodies at late anaphase and translocates to the cytoplasm upon DNA replication stress. Localization to SPBs depends on CDC5 and TEM1 and is inhibited by BUB2. Accumulates | |
Protein Description | Protein kinase of the mitotic exit network (MEN) essential for late nuclear division in the mitotic cycle. Promotes mitotic exit by phosphorylating DBF2 and directly switching on DBF2 kinase activity. Involved in the localization of DBF2 and DBF20 to the neck which is necessary to undergo cytokinesis. Plays a role in segregation of chromosomes during recovery from spindle checkpoint activation. Required for spindle pole localization of CDK1 and inactivation of CDC2 kinase activity at the end of mitosis. Required for spindle disassembly after meiosis II and plays a role in spore morphogenesis.. | |
Protein Sequence | MNSMADTDRVNLTPIQRASEKSVQYHLKQVIGRGSYGVVYKAINKHTDQVVAIKEVVYENDEELNDIMAEISLLKNLNHNNIVKYHGFIRKSYELYILLEYCANGSLRRLISRSSTGLSENESKTYVTQTLLGLKYLHGEGVIHRDIKAANILLSADNTVKLADFGVSTIVNSSALTLAGTLNWMAPEILGNRGASTLSDIWSLGATVVEMLTKNPPYHNLTDANIYYAVENDTYYPPSSFSEPLKDFLSKCFVKNMYKRPTADQLLKHVWINSTENVKVDKLNKFKEDFTDADYHWDADFQEEKLNISPSKFSLAAAPAAWAENNQELDLMPPTESQLLSQLKSSSKPLTDLHVLFSVCSLENIADTIIECLSRTTVDKRLITAFGSIFVYDTQHNHSRLRLKFIAMGGIPLIIKFEHLAKEFVIDYPQTLIECGIMYPPNFASLKTPKYILELVYRFYDLTSTAFWCRWCFKHLDISLLLNNIHERRAQSILLKLSSYAPWSFEKILPSLIDSKLKKKILISPQITYVVFKSINYMITTNDDKIHKSAIPSSSSLPLSSSPTRNSPVNSVQSPSRSPVHSLMATRPSSPMRHKSISNFPHLTISSKSRLLIELPEGFFTWLTSFFVDMAQIKDLSVLKYFTKLCYLTVHINSTFLNDLLDNDAFFAFIRNIDTIIPFIDDAKTAAFIWKQITAICVEMSLDMDQMSASLFSTAMNFIRKKNNTSISGLEIILNCLHFTLRNVNDDVAPTVGSSESHSVFLIKVNNDAAIELPIDQLVDLFYALNDDDVNLSKLISIFTKICSLPGFENLTINIIFHPNFYEKIVSFFDTYFNSLLIQIDLLKFIKLIFSKSLLKLYDYTGQPDPIKQTEPNRRNKATVFKLRAILVQITEFLNNNWNKDVPKRNSNQVGGDSVLICQLCEDIRSLSKKGSLQKVSSVTAAIGSSPTKDERSNLRSSKDKSDGFSVPITTFQT | |
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 |
---|---|---|---|---|---|
7 | Phosphorylation | -MNSMADTDRVNLTP -CCCCCCCCCCCCCH | 19.03 | 30377154 | |
13 | Phosphorylation | DTDRVNLTPIQRASE CCCCCCCCHHHHHCH | 17.09 | 27214570 | |
92 | Phosphorylation | YHGFIRKSYELYILL CCEEECCCHHHHHHH | 17.62 | 27017623 | |
93 | Phosphorylation | HGFIRKSYELYILLE CEEECCCHHHHHHHH | 17.00 | 27017623 | |
96 | Phosphorylation | IRKSYELYILLEYCA ECCCHHHHHHHHHHH | 4.23 | 27017623 | |
101 | Phosphorylation | ELYILLEYCANGSLR HHHHHHHHHHCCHHH | 9.24 | 27017623 | |
106 | Phosphorylation | LEYCANGSLRRLISR HHHHHCCHHHHHHHH | 20.64 | 27017623 | |
119 | Phosphorylation | SRSSTGLSENESKTY HHCCCCCCCCCCHHH | 39.46 | 28889911 | |
123 | Phosphorylation | TGLSENESKTYVTQT CCCCCCCCHHHHHHH | 41.71 | 28889911 | |
222 | Phosphorylation | NPPYHNLTDANIYYA CCCCCCCCCCCEEEE | 38.08 | 19779198 | |
240 | Phosphorylation | DTYYPPSSFSEPLKD CCCCCCCCCCHHHHH | 38.27 | 19779198 | |
242 | Phosphorylation | YYPPSSFSEPLKDFL CCCCCCCCHHHHHHH | 40.01 | 19779198 | |
309 | Phosphorylation | QEEKLNISPSKFSLA CHHHHCCCHHHHCHH | 23.27 | 19823750 | |
311 | Phosphorylation | EKLNISPSKFSLAAA HHHCCCHHHHCHHHC | 39.27 | 19823750 | |
549 | Phosphorylation | NDDKIHKSAIPSSSS CCCHHHHCCCCCCCC | 19.78 | 21126336 | |
560 | Phosphorylation | SSSSLPLSSSPTRNS CCCCCCCCCCCCCCC | 27.16 | 23749301 | |
561 | Phosphorylation | SSSLPLSSSPTRNSP CCCCCCCCCCCCCCC | 48.28 | 28889911 | |
562 | Phosphorylation | SSLPLSSSPTRNSPV CCCCCCCCCCCCCCC | 27.24 | 10837230 | |
564 | Phosphorylation | LPLSSSPTRNSPVNS CCCCCCCCCCCCCCC | 44.42 | 25752575 | |
567 | Phosphorylation | SSSPTRNSPVNSVQS CCCCCCCCCCCCCCC | 27.25 | 23749301 | |
571 | Phosphorylation | TRNSPVNSVQSPSRS CCCCCCCCCCCCCCC | 23.05 | 19779198 | |
574 | Phosphorylation | SPVNSVQSPSRSPVH CCCCCCCCCCCCCCH | 23.76 | 23749301 | |
578 | Phosphorylation | SVQSPSRSPVHSLMA CCCCCCCCCCHHHHC | 35.29 | 28889911 | |
586 | Phosphorylation | PVHSLMATRPSSPMR CCHHHHCCCCCCCCC | 29.19 | 19779198 | |
589 | Phosphorylation | SLMATRPSSPMRHKS HHHCCCCCCCCCCCC | 43.73 | 30377154 | |
590 | Phosphorylation | LMATRPSSPMRHKSI HHCCCCCCCCCCCCC | 25.95 | 25752575 | |
596 | Phosphorylation | SSPMRHKSISNFPHL CCCCCCCCCCCCCCE | 25.73 | 28152593 | |
598 | Phosphorylation | PMRHKSISNFPHLTI CCCCCCCCCCCCEEE | 39.24 | 25752575 | |
604 | Phosphorylation | ISNFPHLTISSKSRL CCCCCCEEECCCCCE | 18.77 | 28889911 | |
606 | Phosphorylation | NFPHLTISSKSRLLI CCCCEEECCCCCEEE | 26.86 | 21551504 | |
607 | Phosphorylation | FPHLTISSKSRLLIE CCCEEECCCCCEEEE | 30.69 | 24961812 | |
870 | Phosphorylation | QPDPIKQTEPNRRNK CCCCCCCCCCCCCCH | 48.70 | 22031224 | |
937 | Phosphorylation | KGSLQKVSSVTAAIG CCCCHHHHHCCHHCC | 26.57 | 24961812 | |
938 | Phosphorylation | GSLQKVSSVTAAIGS CCCHHHHHCCHHCCC | 26.86 | 21440633 | |
945 | Phosphorylation | SVTAAIGSSPTKDER HCCHHCCCCCCCCHH | 27.34 | 25521595 | |
946 | Phosphorylation | VTAAIGSSPTKDERS CCHHCCCCCCCCHHH | 31.23 | 22369663 | |
948 | Phosphorylation | AAIGSSPTKDERSNL HHCCCCCCCCHHHCC | 53.74 | 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 CDC15_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC15_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 CDC15_YEAST !! |
Kegg Drug | ||||||
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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-309; SER-560; SER-562;THR-564; SER-596 AND SER-946, 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-946, AND MASSSPECTROMETRY. | |
"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 SER-562, AND MASSSPECTROMETRY. |