UniProt ID | SPC98_YEAST | |
---|---|---|
UniProt AC | P53540 | |
Protein Name | Spindle pole body component SPC98 | |
Gene Name | SPC98 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 846 | |
Subcellular Localization | Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. | |
Protein Description | Involved in microtubule organization by the microtubule organizing center, the spindle pole body (SPB). Probably part of the microtubule attachment site at the SPB.. | |
Protein Sequence | MELEPTLFGIIEALAPQLLSQSHLQTFVSDVVNLLRSSTKSATQLGPLIDFYKLQSLDSPETTIMWHKIEKFLDALFGIQNTDDMVKYLSVFQSLLPSNYRAKIVQKSSGLNMENLANHEHLLSPVRAPSIYTEASFENMDRFSERRSMVSSPNRYVPSSTYSSVTLRQLSNPYYVNTIPEEDILKYVSYTLLATTSALFPFDHEQIQIPSKIPNFESGLLHLIFEAGLLYQSLGYKVEKFRMLNISPMKKALIIEISEELQNYTAFVNNLVSSGTVVSLKSLYREIYENIIRLRIYCRFTEHLEELSGDTFLIELNIFKSHGDLTIRKIATNLFNSMISLYYEYLMNWLTKGLLRATYGEFFIAENTDTNGTDDDFIYHIPIEFNQERVPAFIPKELAYKIFMIGKSYIFLEKYCKEVQWTNEFSKKYHVLYQSNSYRGISTNFFEIINDQYSEIVNHTNQILNQKFHYRDVVFALKNILLMGKSDFMDALIEKANDILATPSDSLPNYKLTRVLQEAVQLSSLRHLMNSPRNSSVINGLDARVLDLGHGSVGWDVFTLDYILYPPLSLVLNVNRPFGRKEYLRIFNFLWRFKKNNYFYQKEMLKSNDIIRSFKKIRGYNPLIRDIINKLSRISILRTQFQQFNSKMESYYLNCIIEENFKEMTRKLQRTENKSQNQFDLIRLNNGTIELNGILTPKAEVLTKSSSSKPQKHAIEKTLNIDELESVHNTFLTNILSHKLFATNTSEISVGDYSGQPYPTSLVLLLNSVYEFVKVYCNLNDIGYEIFIKMNLNDHEASNGLLGKFNTNLKEIVSQYKNFKDRLYIFRADLKNDGDEELFLLSKSLR | |
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 |
---|---|---|---|---|---|
108 | Phosphorylation | RAKIVQKSSGLNMEN HHHEEHHCCCCCHHH | 16.73 | 28889911 | |
109 | Phosphorylation | AKIVQKSSGLNMENL HHEEHHCCCCCHHHH | 55.10 | 21700874 | |
124 | Phosphorylation | ANHEHLLSPVRAPSI CCCHHHCCCCCCCCC | 27.92 | 21700874 | |
136 | Phosphorylation | PSIYTEASFENMDRF CCCCCHHCCCCCHHH | 27.19 | 28889911 | |
144 | Phosphorylation | FENMDRFSERRSMVS CCCCHHHHHHHHCCC | 30.96 | 21700874 | |
148 | Phosphorylation | DRFSERRSMVSSPNR HHHHHHHHCCCCCCC | 29.74 | 22369663 | |
151 | Phosphorylation | SERRSMVSSPNRYVP HHHHHCCCCCCCCCC | 31.28 | 22369663 | |
152 | Phosphorylation | ERRSMVSSPNRYVPS HHHHCCCCCCCCCCC | 18.13 | 22369663 | |
159 | Phosphorylation | SPNRYVPSSTYSSVT CCCCCCCCCCCCCEE | 25.85 | 28889911 | |
160 | Phosphorylation | PNRYVPSSTYSSVTL CCCCCCCCCCCCEEH | 25.87 | 19779198 | |
164 | Phosphorylation | VPSSTYSSVTLRQLS CCCCCCCCEEHHHCC | 14.54 | 25752575 | |
433 | Phosphorylation | SKKYHVLYQSNSYRG HHHEEEEECCCCCCC | 14.60 | 28132839 | |
438 | Phosphorylation | VLYQSNSYRGISTNF EEECCCCCCCCCCCH | 19.67 | 21700874 | |
510 | Phosphorylation | PSDSLPNYKLTRVLQ CCCCCCCHHHHHHHH | 12.87 | 21700874 | |
524 | Phosphorylation | QEAVQLSSLRHLMNS HHHHHHHHHHHHHCC | 37.71 | 21700874 | |
531 | Phosphorylation | SLRHLMNSPRNSSVI HHHHHHCCCCCHHHH | 15.98 | 21700874 | |
703 | Phosphorylation | TPKAEVLTKSSSSKP CCCEEEECCCCCCCC | 33.77 | 27017623 | |
705 | Phosphorylation | KAEVLTKSSSSKPQK CEEEECCCCCCCCCH | 30.16 | 21700874 | |
708 | Phosphorylation | VLTKSSSSKPQKHAI EECCCCCCCCCHHHH | 50.75 | 27017623 | |
831 | Acetylation | YIFRADLKNDGDEEL EEEEECCCCCCCHHH | 54.24 | 24489116 | |
843 | Ubiquitination | EELFLLSKSLR---- HHHHHEECCCC---- | 54.18 | 24961812 |
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 SPC98_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPC98_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 SPC98_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-124; SER-136; SER-152AND SER-159, AND MASS SPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-151, ANDMASS SPECTROMETRY. |