| UniProt ID | SPC29_YEAST | |
|---|---|---|
| UniProt AC | P33419 | |
| Protein Name | Spindle pole component 29 | |
| Gene Name | SPC29 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 253 | |
| Subcellular Localization | Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . | |
| Protein Description | Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Links the central plaque component SPC42 to the inner plaque component SPC110.. | |
| Protein Sequence | MDYSNFGNSASKKFQDDTLNRVRKEHEEALKKLREENFSSNTSELGNKKHYRAQERMSSPLHRLSPTGKSDDRKVKSPLDDKLRRQLREGNTRLPPPPFSSYGMPPTNRSNLDRIRRRTSSPVRTDKFASQNVIDDQRLEIKYLERIVYDQGTVIDNLTSRITRLESFILNSISDRGDKNFASLEHSRSFSGFPTNKTYGLQMGGLYENDMPYRRSSDNINKEGAREDRSSQIHIENESTEDILKILSSSFHN | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MDYSNFGNSAS ----CCCCCCCCCHH | 22.78 | 28889911 | |
| 9 | Phosphorylation | DYSNFGNSASKKFQD CCCCCCCCHHHHHHH | 34.01 | 21700874 | |
| 11 | Phosphorylation | SNFGNSASKKFQDDT CCCCCCHHHHHHHHH | 35.88 | 28152593 | |
| 18 | Phosphorylation | SKKFQDDTLNRVRKE HHHHHHHHHHHHHHH | 33.93 | 19823750 | |
| 39 | Phosphorylation | KLREENFSSNTSELG HHHHHCCCCCHHHHC | 33.97 | 23607784 | |
| 40 | Phosphorylation | LREENFSSNTSELGN HHHHCCCCCHHHHCC | 39.73 | 21440633 | |
| 42 | Phosphorylation | EENFSSNTSELGNKK HHCCCCCHHHHCCHH | 26.06 | 25521595 | |
| 43 | Phosphorylation | ENFSSNTSELGNKKH HCCCCCHHHHCCHHH | 34.77 | 19823750 | |
| 51 | Phosphorylation | ELGNKKHYRAQERMS HHCCHHHHHHHHHHC | 19.27 | 24961812 | |
| 58 | Phosphorylation | YRAQERMSSPLHRLS HHHHHHHCCCHHHCC | 34.72 | 22369663 | |
| 59 | Phosphorylation | RAQERMSSPLHRLSP HHHHHHCCCHHHCCC | 23.34 | 22369663 | |
| 65 | Phosphorylation | SSPLHRLSPTGKSDD CCCHHHCCCCCCCCC | 22.00 | 22369663 | |
| 67 | Phosphorylation | PLHRLSPTGKSDDRK CHHHCCCCCCCCCCC | 54.59 | 22369663 | |
| 70 | Phosphorylation | RLSPTGKSDDRKVKS HCCCCCCCCCCCCCC | 46.19 | 28889911 | |
| 77 | Phosphorylation | SDDRKVKSPLDDKLR CCCCCCCCCCCHHHH | 33.41 | 19823750 | |
| 100 | Phosphorylation | RLPPPPFSSYGMPPT CCCCCCCHHCCCCCC | 28.55 | 21700874 | |
| 102 | Phosphorylation | PPPPFSSYGMPPTNR CCCCCHHCCCCCCCC | 19.08 | 21700874 | |
| 107 | Phosphorylation | SSYGMPPTNRSNLDR HHCCCCCCCCCHHHH | 37.08 | 21700874 | |
| 119 | Phosphorylation | LDRIRRRTSSPVRTD HHHHHHHCCCCCCCC | 31.57 | 28889911 | |
| 120 | Phosphorylation | DRIRRRTSSPVRTDK HHHHHHCCCCCCCCC | 30.73 | 27214570 | |
| 121 | Phosphorylation | RIRRRTSSPVRTDKF HHHHHCCCCCCCCCH | 27.14 | 27214570 | |
| 125 | Phosphorylation | RTSSPVRTDKFASQN HCCCCCCCCCHHHCC | 43.72 | 21700874 | |
| 130 | Phosphorylation | VRTDKFASQNVIDDQ CCCCCHHHCCCCCCH | 25.97 | 21700874 | |
| 163 | Phosphorylation | DNLTSRITRLESFIL HHHHHHHHHHHHHHH | 28.26 | 21700874 | |
| 167 | Phosphorylation | SRITRLESFILNSIS HHHHHHHHHHHHHCC | 23.37 | 19795423 | |
| 172 | Phosphorylation | LESFILNSISDRGDK HHHHHHHHCCCCCCC | 21.74 | 19795423 | |
| 174 | Phosphorylation | SFILNSISDRGDKNF HHHHHHCCCCCCCCC | 22.52 | 19795423 | |
| 183 | Phosphorylation | RGDKNFASLEHSRSF CCCCCCHHHCCCCCC | 30.10 | 19795423 | |
| 187 | Phosphorylation | NFASLEHSRSFSGFP CCHHHCCCCCCCCCC | 21.90 | 25704821 | |
| 189 | Phosphorylation | ASLEHSRSFSGFPTN HHHCCCCCCCCCCCC | 27.12 | 22369663 | |
| 191 | Phosphorylation | LEHSRSFSGFPTNKT HCCCCCCCCCCCCCC | 40.55 | 22369663 | |
| 195 | Phosphorylation | RSFSGFPTNKTYGLQ CCCCCCCCCCCCCCC | 47.27 | 21440633 | |
| 207 | Phosphorylation | GLQMGGLYENDMPYR CCCCCCCCCCCCCCC | 18.89 | 24961812 | |
| 213 | Phosphorylation | LYENDMPYRRSSDNI CCCCCCCCCCCCCCC | 16.42 | 20377248 | |
| 216 | Phosphorylation | NDMPYRRSSDNINKE CCCCCCCCCCCCCCC | 32.80 | 20377248 | |
| 217 | Phosphorylation | DMPYRRSSDNINKEG CCCCCCCCCCCCCCC | 32.63 | 20377248 | |
| 230 | Phosphorylation | EGAREDRSSQIHIEN CCCCCCCCCCEEECC | 38.63 | 21700874 | |
| 231 | Phosphorylation | GAREDRSSQIHIENE CCCCCCCCCEEECCC | 33.76 | 21700874 | |
| 239 | Phosphorylation | QIHIENESTEDILKI CEEECCCCHHHHHHH | 48.99 | 22369663 | |
| 240 | Phosphorylation | IHIENESTEDILKIL EEECCCCHHHHHHHH | 31.34 | 22369663 | |
| 249 | Phosphorylation | DILKILSSSFHN--- HHHHHHHHHCCC--- | 33.31 | 22369663 | |
| 250 | Phosphorylation | ILKILSSSFHN---- HHHHHHHHCCC---- | 27.44 | 20377248 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 240 | T | Phosphorylation | Kinase | MPS1 | P54199 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 240 | T | Phosphorylation |
| 19269975 |
* 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 SPC29_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 THR-18; SER-189 AND THR-240,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 THR-18; SER-43; SER-59;SER-65; SER-216 AND THR-240, AND MASS SPECTROMETRY. | |
| "Budding yeast centrosome duplication requires stabilization of Spc29via Mps1-mediated phosphorylation."; Holinger E.P., Old W.M., Giddings T.H. Jr., Wong C., Yates J.R. III,Winey M.; J. Biol. Chem. 284:12949-12955(2009). Cited for: PHOSPHORYLATION AT THR-240, MUTAGENESIS OF THR-240, MASS SPECTROMETRY,AND FUNCTION. | |
