UniProt ID | SPC42_YEAST | |
---|---|---|
UniProt AC | P36094 | |
Protein Name | Spindle pole body component SPC42 | |
Gene Name | SPC42 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 363 | |
Subcellular Localization | Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . | |
Protein Description | Forms a polymeric layer at the periphery of the spindle pole body (SPB) central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane.. | |
Protein Sequence | MNGSPTPKRYSSKSSRLYDDYYNIPYQYSNPTPMNRDYNDVGSRINADKLVPEEYKRNTEFINKAVQQNKELNFKLREKQNEIFELKKIAETLRSKLEKYVDITKKLEDQNLNLQIKISDLEKKLSDANSTFKEMRFPKVKDPMVDDDPVSENYDQINVPKHRAPDATGNPRTTNKVSNTSDQDSRLKAIERTLSVLTNYVMRSEDGNNDRMSPLPSPLNTILPINNRLNFQEPKRYNPTVKVNPSDDDIMMYESAELKRVEEEIEELKRKILVRKKHDLRKLSLNNQLQELQSMMDGDDNIKLDNVSKHNHATHRHSSQSSRDYSPSSDACLECSNDLYEKNRVKPENNMSETFATPTPNNR | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MNGSPTPKRYS ----CCCCCCCCCCC | 22.16 | 24909858 | |
6 | Phosphorylation | --MNGSPTPKRYSSK --CCCCCCCCCCCCC | 43.04 | 28889911 | |
12 | Phosphorylation | PTPKRYSSKSSRLYD CCCCCCCCCCCCCCC | 27.85 | 17563356 | |
13 | Acetylation | TPKRYSSKSSRLYDD CCCCCCCCCCCCCCC | 46.65 | 23572591 | |
28 | Phosphorylation | YYNIPYQYSNPTPMN CCCCCCCCCCCCCCC | 12.46 | 21700874 | |
29 | Phosphorylation | YNIPYQYSNPTPMNR CCCCCCCCCCCCCCC | 22.32 | 21700874 | |
32 | Phosphorylation | PYQYSNPTPMNRDYN CCCCCCCCCCCCCCC | 39.15 | 21440633 | |
43 | Phosphorylation | RDYNDVGSRINADKL CCCCCHHHHCCHHHC | 29.81 | 21700874 | |
59 | Phosphorylation | PEEYKRNTEFINKAV CHHHHHCHHHHHHHH | 35.98 | 25704821 | |
92 | Phosphorylation | ELKKIAETLRSKLEK HHHHHHHHHHHHHHH | 20.60 | 21700874 | |
95 | Phosphorylation | KIAETLRSKLEKYVD HHHHHHHHHHHHHHH | 44.71 | 21700874 | |
104 | Phosphorylation | LEKYVDITKKLEDQN HHHHHHHHHHHHHCC | 20.05 | 27017623 | |
126 | Phosphorylation | SDLEKKLSDANSTFK HHHHHHHHHCCCHHH | 43.48 | 30377154 | |
130 | Phosphorylation | KKLSDANSTFKEMRF HHHHHCCCHHHHCCC | 36.62 | 21700874 | |
131 | Phosphorylation | KLSDANSTFKEMRFP HHHHCCCHHHHCCCC | 38.23 | 21700874 | |
151 | Phosphorylation | MVDDDPVSENYDQIN CCCCCCCCCCCHHCC | 26.05 | 20377248 | |
154 | Phosphorylation | DDPVSENYDQINVPK CCCCCCCCHHCCCCC | 12.74 | 22369663 | |
168 | Phosphorylation | KHRAPDATGNPRTTN CCCCCCCCCCCCCCC | 44.89 | 21700874 | |
176 | Ubiquitination | GNPRTTNKVSNTSDQ CCCCCCCCCCCCCCH | 44.97 | 23749301 | |
185 | Phosphorylation | SNTSDQDSRLKAIER CCCCCHHHHHHHHHH | 33.60 | 23749301 | |
193 | Phosphorylation | RLKAIERTLSVLTNY HHHHHHHHHHHHHHH | 15.59 | 30377154 | |
195 | Phosphorylation | KAIERTLSVLTNYVM HHHHHHHHHHHHHHH | 17.92 | 28152593 | |
204 | Phosphorylation | LTNYVMRSEDGNNDR HHHHHHHCCCCCCCC | 23.19 | 22369663 | |
213 | Phosphorylation | DGNNDRMSPLPSPLN CCCCCCCCCCCCCHH | 24.95 | 22369663 | |
217 | Phosphorylation | DRMSPLPSPLNTILP CCCCCCCCCHHHCEE | 50.10 | 22369663 | |
221 | Phosphorylation | PLPSPLNTILPINNR CCCCCHHHCEEECCC | 31.41 | 22369663 | |
246 | Phosphorylation | PTVKVNPSDDDIMMY CCCCCCCCCCCCCHH | 48.76 | 21700874 | |
253 | Phosphorylation | SDDDIMMYESAELKR CCCCCCHHHHHHHHH | 6.86 | 21700874 | |
255 | Phosphorylation | DDIMMYESAELKRVE CCCCHHHHHHHHHHH | 15.00 | 21700874 | |
284 | Phosphorylation | KHDLRKLSLNNQLQE HHHHHHHHHHHHHHH | 31.89 | 22369663 | |
294 | Phosphorylation | NQLQELQSMMDGDDN HHHHHHHHHHCCCCC | 28.79 | 21700874 | |
308 | Phosphorylation | NIKLDNVSKHNHATH CEECCCHHHCCCCCC | 34.16 | 21440633 | |
318 | Phosphorylation | NHATHRHSSQSSRDY CCCCCCCCCCCCCCC | 29.99 | 21700874 | |
319 | Phosphorylation | HATHRHSSQSSRDYS CCCCCCCCCCCCCCC | 28.14 | 21700874 | |
321 | Phosphorylation | THRHSSQSSRDYSPS CCCCCCCCCCCCCCC | 29.32 | 21700874 | |
322 | Phosphorylation | HRHSSQSSRDYSPSS CCCCCCCCCCCCCCC | 22.87 | 23749301 | |
325 | Phosphorylation | SSQSSRDYSPSSDAC CCCCCCCCCCCCHHH | 22.75 | 23749301 | |
326 | Phosphorylation | SQSSRDYSPSSDACL CCCCCCCCCCCHHHH | 23.69 | 27738172 | |
328 | Phosphorylation | SSRDYSPSSDACLEC CCCCCCCCCHHHHHC | 34.60 | 27214570 | |
329 | Phosphorylation | SRDYSPSSDACLECS CCCCCCCCHHHHHCC | 32.39 | 27214570 | |
336 | Phosphorylation | SDACLECSNDLYEKN CHHHHHCCHHHHHHC | 24.81 | 21700874 | |
342 | Ubiquitination | CSNDLYEKNRVKPEN CCHHHHHHCCCCCCC | 36.18 | 23749301 | |
346 | Ubiquitination | LYEKNRVKPENNMSE HHHHCCCCCCCCCCC | 43.29 | 23749301 | |
352 | Phosphorylation | VKPENNMSETFATPT CCCCCCCCCCCCCCC | 35.29 | 29136822 | |
354 | Phosphorylation | PENNMSETFATPTPN CCCCCCCCCCCCCCC | 15.97 | 29136822 | |
357 | Phosphorylation | NMSETFATPTPNNR- CCCCCCCCCCCCCC- | 24.41 | 22369663 | |
359 | Phosphorylation | SETFATPTPNNR--- CCCCCCCCCCCC--- | 34.00 | 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 SPC42_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPC42_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 SPC42_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-284 AND SER-326, ANDMASS 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-12, 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-213 AND SER-217, ANDMASS SPECTROMETRY. |